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Information on EC 2.7.7.101 - DNA primase DnaG
for references in articles please use BRENDA:EC2.7.7.101
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.7 Nucleotidyltransferases
2.7.7.101 DNA primase DnaG
IUBMB Comments
The enzyme catalyses the synthesis of short RNA sequences that are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase. It is found in bacteria and archaea. The latter also have a second primase system (EC 2.7.7.102, DNA primase AEP).
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
- 2.7.7.101
- helicase
-
fork
- primases
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replisome
- dnab
- suramin
- solfataricus
- drug development
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sulfolobus
-
primosome
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unwind
Reaction Schemes
show+
n
=
ssDNA/pppN(pN)n-1 hybrid
+
(n-1)
Synonyms
primase dnag, ssodnag, dna primase dnag, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DNA primase
DnaG
DnaG primase
DnaG primase-A
Mtb DnaG primase
primase DnaG
Sso0079
DnaG
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
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SYSTEMATIC NAME
IUBMB Comments
nucleotide 5'-triphosphate:single-stranded DNA nucleotidyltransferase (DNA-RNA hybrid synthesizing)
The enzyme catalyses the synthesis of short RNA sequences that are used as primers for EC 2.7.7.7, DNA-directed DNA polymerase. It is found in bacteria and archaea. The latter also have a second primase system (EC 2.7.7.102, DNA primase AEP).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
bacteriophage alpha3 ssDNA + n NTP
bacteriophage alpha3 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
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Substrates: -
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bacteriophage alpha3 ssDNA + n rNTP
bacteriophage alpha3 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
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Substrates: -
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bacteriophage G4 ssDNA + n rNTP
bacteriophage G4 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
bacteriophage M13 ssDNA + n NTP
bacteriophage M13 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
bacteriophage phiK ssDNA + n rNTP
bacteriophage phiK ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
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bacteriophage ST-1 ssDNA + n rNTP
bacteriophage ST-1 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
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bacteriophage G4 ssDNA + n rNTP
bacteriophage G4 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
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Substrates: -
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bacteriophage G4 ssDNA + n rNTP
bacteriophage G4 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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bacteriophage M13 ssDNA + n NTP
bacteriophage M13 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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bacteriophage M13 ssDNA + n NTP
bacteriophage M13 ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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NTP + n NTP
N(pN)n + n diphosphate
Substrates: -
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NTP + n NTP
N(pN)n + n diphosphate
Substrates: SsoDnaG is only able to utilize NTPs and not dNTPs (in contrast to the heterodimeric eukaryotic DNA primases from archaea are able to incorporate either NTP or dNTP substrates to synthesize RNA, DNA, or hybrid primer products). Slightly positive cooperativity for binding at least two SsoDnaG molecules to DNA. SsoDnaG shows greater than fourfold faster rate of DNA priming over that of eukaryotic-type primase under optimal in vitro conditions. Incorporation of NTPs leads to the formation of primer products that ranged from 2 to 15 nucleotides. Dimer, 4 mer, and 13 mer products are primarily produced
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
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Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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additional information
?
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Substrates: the DnaG protein can use ADP in place of ATP. Primer formation by DnaG protein is strictly stoichiometric in vitro, one molecule of dnaG protein is required to prime one molecule of alpha3 DNA. The site recognized by DnaG protein on alpha3 DNA in vitro is within the same region of the alpha3 chromosome as the origin of replication in vivo
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additional information
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Substrates: in all four phages studied, the negative strand initiation site occurs within an intercistronic region of approximately 135 bases. Extensive nucleotide conservation exists at the negative strand origin. The conserved origin DNA occurs in two regions, 42 and 45 bases long, which are separated by 13 bases of divergent sequence. The start point of negative strand synthesis lies just prior to one of these hairpins correlated with the two stretches of conserved nucleotide sequence
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additional information
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Substrates: other single-stranded and duplex DNA templates tested are inactive
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additional information
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Substrates: enzyme recombineering efficiency assay via gene deletion
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additional information
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Substrates: enzyme recombineering efficiency assay via gene deletion
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additional information
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Substrates: Escherichia coli DnaG may utilize 2',3'-dideoxynucleoside 5'-triphosphates (ddNTPs) as substrates
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additional information
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Substrates: enzyme initiates at 3'-ATC-5' and 3'-ATT-5' sites synthesizing primers that are 22 or 23 nucleotides long
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additional information
?
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Substrates: the archaeal DnaG binds to the Csl4-exosome but not to the Rrp4-exosome of Sulfolobus solfataricus. DnaG modulates the substrate specificity of the Csl4-exosome
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additional information
?
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Substrates: the enzyme exhibits primase activity in vitro
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NTP + n NTP
N(pN)n + n diphosphate
Substrates: -
Products: -
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additional information
?
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Substrates: the archaeal DnaG binds to the Csl4-exosome but not to the Rrp4-exosome of Sulfolobus solfataricus. DnaG modulates the substrate specificity of the Csl4-exosome
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
-
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
Products: -
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ssDNA + n NTP
ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate
Substrates: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
either Mg2+ or Mn2+ stimulates primer formation over that without any metals or Zn2+. A combination of both Mg2+ and Mn2+ does not stimulate further primer synthesis over that of the single metal Mn2+
Mn2+
either Mg2+ or Mn2+ stimulates primer formation over that without any metals or Zn2+. A combination of both Mg2+ and Mn2+ does not stimulate further primer synthesis over that of the single metal Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(7S)-7-[(2R,4S,5R,6R)-4-amino-5-hydroxy-6-methyloxan-2-yl]oxy-9-ethyl-6,9,11-trihydroxy-8,10-dihydro-7H-tetracene-5,12-dione
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(7S,9S)-9-acetyl-7-[(2R,4S,5S,6S)-4-amino-5-hydroxy-6-methyloxan-2-yl] oxy-6,9,11-trihydroxy-4-methoxy-8,10-dihydro-7H-tetracene-5,12-dione
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1-(3-((3-(o-tolyl)-1,2,4-oxadiazol-5-yl)methyl)piperidin-1-yl)-2-(3-(trifluoromethyl)phenyl)ethan-1-one
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1-(4-methyl-2-nitrophenoxy)-3-[4-(3-phenyl-1,2,4-thiadiazol-5-yl)piperazino]propan-2-ol
-
2'-deoxy-2'-azidocytidine 5'-triphosphate
pronounced inhibition, not reversed by presence of dCTP or CTP. Inhibitor is incorporated into the primer and terminates the extension of the primer strand
doxorubicin
contains aromatic structure with polar functional groups and is a potent (low-mM) DNA and nucleotide triphosphate competitive inhibitor, interacts with more than one site on Mycobacterium tuberculosis DnaG in order to block DNA and/or NTP binding
suramin
contains aromatic structure with polar functional groups and is a potent (low-mM) DNA and nucleotide triphosphate competitive inhibitor, interacts with more than one site on Mycobacterium tuberculosis DnaG in order to block DNA and/or NTP binding
[4-(5-anilino-1,2,4-thiadiazol-3-yl)-3-methyl-1H-pyrazol-1-yl](phenyl)methanone
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3-[2-(ethoxycarbonyl)-5-nitro-1H-indol-3-yl]propanoic acid
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benzo[d]imidazo[2,1-b]imidazole
lead structure for inhibitor search
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benzo[d]imidazo[2,1-b]imidazole
lead structure for inhibitor search
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benzo[d]imidazo[2,1-b]imidazole
lead structure for inhibitor search
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benzo[d]pyrimido[5,4-b]furan
lead structure for inhibitor search
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ppGpp
inhibitory, impedes primase activity by blocking entry of an incoming NTP, and interfering with the binding of either an initiating 5'-NTP, or the extensible 3'-end of an RNA-DNA heteroduplex
ppGpp
inhibitory, impedes primase activity by blocking entry of an incoming NTP, and interfering with the binding of either an initiating 5'-NTP, or the extensible 3'-end of an RNA-DNA heteroduplex
pppGpp
inhibitory, impedes primase activity by blocking entry of an incoming NTP, and interfering with the binding of either an initiating 5'-NTP, or the extensible 3'-end of an RNA-DNA heteroduplex
pppGpp
inhibitory, impedes primase activity by blocking entry of an incoming NTP, and interfering with the binding of either an initiating 5'-NTP, or the extensible 3'-end of an RNA-DNA heteroduplex
pyrido[3',2'4,5]thieno[3,2-d]pyrimidine
lead structure for inhibitor search
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pyrido[3',2'4,5]thieno[3,2-d]pyrimidine
lead structure for inhibitor search
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pyrido[3',2'4,5]thieno[3,2-d]pyrimidine
lead structure for inhibitor search
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additional information
STD-NMR is used to demonstrate binding of one hit to other SSB-Ct binding partners, confirming the possibility of simultaneous inhibition of multiple protein/SSB interactions. The fragment molecules represent promising scaffolds on which to build to discover antibacterial compounds, molecular docking, overview. Structures of hits with binding affinities for further optimization
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additional information
inhibitor screening, three-dimensional pharmacophore development suggests inhibitors that contain two hydrophobes, two hydrogen bond acceptors, and a donor group
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additional information
inhibitor screening, molecular dynamics simulation analysis, and docking and binding affinities, overview. Lys101, Glu137, and Asp188 are identified as the leading amino acids involved in the hydrogen bonding that constituted the few active site residues
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additional information
high-throughput NMR ligand affinity screen of the Staphylococcus aureus primase CTD. Acycloguanosine, adenosine, and myricetin bind poorly to the enzyme's C-terminal domain. Measurement of protein chemical shift perturbations (CSPs), the KD's are greater than 4 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DnaC helicase
DnaG primase is stimulated by the homohexameric DnaB helicase, termed DnaC helicase in Staphylococcus aureus
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DnaB
interaction with the replisome, overview. Analysis of the DnaB N-terminal domain structure and conformations, with or without bound DNA, kinetics. Binding of primase does not inhibit DnaB helicase activity
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DnaB
analysis of the DnaB N-terminal domain structure and conformations, with or without bound DNA, kinetics. In a crystal structure of the Geobacillus stearothermophilus DnaB6-(DnaGC)3 complex, the three C-terminal domains of primase each bind to two adjacent subunits of the dilated N-tier of DnaB. Binding of primase does not inhibit DnaB helicase activity
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DnaB
DnaG is activated about 5000fold when bound to DnaB
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
A novel non-radioactive primase-pyrophosphatase activity assay and its application to the discovery of inhibitors of Mycobacterium tuberculosis primase DnaG.
Tuberculosis
Antimycobacterial activity of DNA intercalator inhibitors of Mycobacterium tuberculosis primase DnaG.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.085
NTP
KM-value is determined by measuring the priming rate at different concentrations of NTPs, 70°C, pH 8.5, 1 mM Mn2+, in presence of M13 ssDNA as template, wild-type enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00055
NTP
KM-value is determined by measuring the priming rate at different concentrations of NTPs, 70°C, pH 8.5, in presence of M13 ssDNA as template, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000033
NTP
KM-value is determined by measuring the priming rate at different concentrations of NTPs, 70°C, pH 8.5, in presence of M13 ssDNA as template, mutant enzyme E175Q
0.0063
NTP
KM-value is determined by measuring the priming rate at different concentrations of NTPs, 70°C, pH 8.5, 1 mM Mn2+, in presence of M13 ssDNA as template, wild-type enzyme
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 90
50°C: about 45% of maximal activity, 90°C: about 35% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
phylogenetic analysis of DnaG proteins in archaea, overview
evolution
the archaeal DnaG protein as a bacterial type primase is based on its central TOPRIM domain
evolution
enzyme structure comparisons and phylogenetic analysis
evolution
functional conservation despite the low sequence homology of the DnaB-binding domains of DnaGs of eubacteria. MtDnaB-NTD showed micromolar affinity with DnaG-CTDs from Escherichia coli and Helicobacter pylori and unstable binding with DnaG-CTD from Vibrio cholerae. The interacting domains of both DnaG and DnaB demonstrate the species-specific evolution of the replication initiation system
evolution
sequence and structural homology of DnaG-like primases, overview
evolution
sequence and structural homology of DnaG-like primases, overview
evolution
sequence and structural homology of DnaG-like primases, overview
evolution
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sequence and structural homology of DnaG-like primases, overview
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evolution
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sequence and structural homology of DnaG-like primases, overview
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evolution
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functional conservation despite the low sequence homology of the DnaB-binding domains of DnaGs of eubacteria. MtDnaB-NTD showed micromolar affinity with DnaG-CTDs from Escherichia coli and Helicobacter pylori and unstable binding with DnaG-CTD from Vibrio cholerae. The interacting domains of both DnaG and DnaB demonstrate the species-specific evolution of the replication initiation system
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evolution
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sequence and structural homology of DnaG-like primases, overview
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evolution
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functional conservation despite the low sequence homology of the DnaB-binding domains of DnaGs of eubacteria. MtDnaB-NTD showed micromolar affinity with DnaG-CTDs from Escherichia coli and Helicobacter pylori and unstable binding with DnaG-CTD from Vibrio cholerae. The interacting domains of both DnaG and DnaB demonstrate the species-specific evolution of the replication initiation system
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malfunction
inhibition of primase activity is expected to selectively halt bacterial DNA replication. Halting DNA replication probably has a bacteriocidal effect
malfunction
inhibition of primase activity is expected to selectively halt bacterial DNA replication. Halting DNA replication probably has a bacteriocidal effect
malfunction
inhibition of primase activity is expected to selectively halt bacterial DNA replication. Halting DNA replication probably has a bacteriocidal effect
malfunction
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inhibition of primase activity is expected to selectively halt bacterial DNA replication. Halting DNA replication probably has a bacteriocidal effect
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malfunction
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inhibition of primase activity is expected to selectively halt bacterial DNA replication. Halting DNA replication probably has a bacteriocidal effect
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malfunction
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inhibition of primase activity is expected to selectively halt bacterial DNA replication. Halting DNA replication probably has a bacteriocidal effect
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metabolism
since Sulfolobus solfataricus also harbors a eukaryotic-type primase consisting of two subunits, the organism might use a dual system of primases. Strong association of DnaG with the exosome suggests that this protein plays an important role in RNA metabolism in the third domain of life. The archaeal RNA-degrading exosome contains a catalytically active hexameric core, an RNA-binding cap formed by Rrp4 and Csl4 and the protein annotated as DnaG, a bacterial type primase, with functions in RNA metabolism. Archaeal exosome structure, overview
metabolism
CLC-helicase affinity increases about 500fold upon DnaGC binding, binding mechanism involving DNA, overview
metabolism
CLC-helicase affinity increases about 500fold upon DnaGC binding, binding mechanism involving DNA, overview
physiological function
beside its activity as primase, DnaG is also a poly(A)-binding protein enhancing the degradation of adenine-rich transcripts by the Csl4-exosome, overview. DnaG is the second poly(A)-binding protein besides Rrp4 in the heteromeric, RNA-binding cap of the Sulfolobus solfataricus exosome. DnaG modulates the substrate specificity of the Csl4-exosome. The DnaG-Csl4-exosome degrades MCS-RNA with lower efficiency than the Csl4-exosome, while poly(A) RNA is degraded with higher efficiency. DnaG confers poly(A) specificity to the Csl4-exosome
physiological function
enzyme DnaG strongly binds native and in vitro transcribed rRNA and enables its polynucleotidylation by the exosome. The N-terminal domain of DnaG is a RNA-binding domain with poly(rA)-preference cooperating with the TOPRIM domain in binding of RNA. The C-terminal domain, but not the N-terminal domain, of DnaG is important for the interaction with the exosome. rRNA-derived transcripts with heteropolymeric tails are degraded faster by the exosome than their non-tailed variants
physiological function
a mutation in dnaG causes a block in the synthesis of both leading and lagging strands after initiation, which results in the accumulation of early replicative intermediates. The DnaG protein functions in lagging strand synthesis and may be necessary for the continuation of leading strand synthesis as well
physiological function
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a temperature-sensitive DnaG mutant does not permit normal bacteriophage T4 growth and a normal rate of DNA synthesis. The phage gene 61 RNA primase and the host DnaG primase act independently of each other
physiological function
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bacterial DnaG-type primases, small primase-like proteins from bacteria and archaea, type IA and type II topoisomerases, bacterial and archaeal nucleases of the OLD family and bacterial DNA repair proteins of the RecR/M family contain a common topoisomerase-primase domain, designated Toprim. The domain consists of about 100 amino acids and has two conserved motifs, one of which centers at a onserved glutamate and the other one at two conserved aspartates (DxD)
physiological function
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comparison of the amino acid sequences of primases and associated helicases involved in the DNA replication of eubacteria and bacteriophages T7, T3, T4, P4, and P22. Primases and primase-helicase proteins contain, close to their N-termini, a conserved Zn-finger and encompass five other conserved motifs
physiological function
DnaB helicase and the C-terminal domain of the DnaG primase interact in a six to three ratio to give a complex of 387000 Da. Binding of DnaG leads to changes in the interaction interface
physiological function
DnaG binds to the Csl4 RNA-degrading exosome but not to the Rrp4-exosome of Saccharolobus solfataricus. DnaG is a poly(A)-binding protein enhancing the degradation of adenine-rich transcripts by the Csl4-exosome
physiological function
DnaG interacts with the flexible linker that connects the N- and C-terminal domains of helicase DnaB. Binding of the primase to the helicase induces predominantly a 3fold symmetric morphology to the hexameric ring. Three DnaG molecules interact with the hexameric ring helicase, with a small number of complexes with two and even one DnaG molecule bound to DnaB also detected
physiological function
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DnaG physically interacts with bacteriophage SPP1 hexameric helicase G40P (G40P6) in the absence of ATP. The presence of DnaG in the reaction mixture increases the helicase activity of G40P6 about 3fold, but not the ATPase activity
physiological function
error-prone DNA polymerase DnaEBs interacts with the replicative helicase DnaC and primase DnaG in a ternary complex. The DnaG-DnaEBs hand-off takes place after de novo polymerization of only two ribonucleotides by DnaG, and does not require other replication proteins. The fidelity of DnaEBs is improved by DnaC and DnaG
physiological function
in the presence of the helicase DnaB the size distribution of primers is different, and a range of additional smaller primers are also synthesized. Mutations E15A, Y88A, and E15A Y88A in DnaB bind DnaG but are not able to modulate primer size, whereas the R195A/M196A mutant inhibits the primase activity
physiological function
-
model of the RNA polymerase domain bound to the primed template. As the template strand exits the binding site on the primase on the 5'-side it enters the active site of the DNA polymerase in a proper polarity
physiological function
the interaction of single-stranded DNA-binding protein SSB and primase is mediated by the C-terminus of SSB. An array of conserved amino acids on DnaG C-terminus forms a hydrophobic pocket surrounded by basic residues, involved in the interaction with SSB
physiological function
DnaG is a DNA-dependent RNA polymerase. In bacteria, the DnaG primase is responsible for synthesis of short RNA primers used to initiate chain extension by replicative DNA polymerase(s) during chromosomal replication. Among the proteins with which Escherichia coli DnaG interacts is the single-stranded DNA-binding protein, SSB. SSB protects single-stranded DNA during DNA replication
physiological function
DnaG primase is stimulated by the homohexameric DnaB helicase, termed DnaC helicase in Staphylococcus aureus. DnaC helicase /DnaB helicase dissociates the two strands of duplex DNA during DNA replication while hydrolyzing ATP, and travels processively in the 5'-3' direction along the single-stranded lagging template toward the replication fork, communicating allosterically with the multi-subunit replicative DNA polymerase. This action keeps it in proximity of the replication fork and ensures the primers are synthesized on the exposed single-stranded DNA nearest to the replication fork. Since primase activity is weak, the stimulation by DnaB causes primase to synthesize primers only at the replication fork when and where they are needed
physiological function
during DNA replication in Escherichia coli, a switch between DnaG primase and DNA polymerase III holoenzyme (pol III) activities has to occur every time when the synthesis of a new Okazaki fragment starts. As both primase and the chi subunit of pol III interact with the highly conserved C-terminus of single-stranded DNA-binding protein (SSB), it is proposed that the binding of both proteins to SSB is mutually exclusive. The addition of pol III does not lead to a displacement of primase, but to the formation of higher complexes. Even pol III-mediated primer elongation by one or several DNA nucleotides does not result in the dissociation of DnaG. The concurrent binding of primase and pol III is highly plausible, since even the SSB tetramer situated directly next to the 3'-terminus of the primer provides four C-termini for protein-protein interactions
physiological function
the bacterial primase is an essential component in the replisome, molecular mechanisms at the DNA replication apparatus, overview
physiological function
the bacterial primase is an essential component in the replisome, molecular mechanisms at the DNA replication apparatus, overview
physiological function
the bacterial primase is an essential component in the replisome, molecular mechanisms at the DNA replication apparatus, overview
physiological function
the helicase-primase interaction is an essential event in DNA replication and is mediated by the highly variable C-terminal domain (CTD) of primase (DnaG) and N-terminal domain (NTD) of helicase (DnaB)
physiological function
the primase-induced conformational switch controls the stability of the bacterial replisome. The dynamic interaction of the Escherichia coli DnaG primase and DnaB helicase affects the stability of the replisome and the cycling of DNA polymerase III complexes at the replication fork through a conformational switch in DnaB that toggles its affinity for the polymerase. Molecular mechanism for polymerase exchange and revised model for the replication reaction that emphasizes its stochasticity, overview. DnaG stimulates polymerase accumulation and slows its exchange at the replication fork
physiological function
the primase-induced conformational switch controls the stability of the bacterial replisome. The dynamic interaction of the Escherichia coli DnaG primase and DnaB helicase affects the stability of the replisome and the cycling of DNA polymerase III complexes at the replication fork through a conformational switch in DnaB that toggles its affinity for the polymerase. Molecular mechanism for polymerase exchange and revised model for the replication reaction that emphasizes its stochasticity, overview. DnaG stimulates polymerase accumulation and slows its exchange at the replication fork
physiological function
-
error-prone DNA polymerase DnaEBs interacts with the replicative helicase DnaC and primase DnaG in a ternary complex. The DnaG-DnaEBs hand-off takes place after de novo polymerization of only two ribonucleotides by DnaG, and does not require other replication proteins. The fidelity of DnaEBs is improved by DnaC and DnaG
-
physiological function
-
the bacterial primase is an essential component in the replisome, molecular mechanisms at the DNA replication apparatus, overview
-
physiological function
-
DnaB helicase and the C-terminal domain of the DnaG primase interact in a six to three ratio to give a complex of 387000 Da. Binding of DnaG leads to changes in the interaction interface
-
physiological function
-
model of the RNA polymerase domain bound to the primed template. As the template strand exits the binding site on the primase on the 5'-side it enters the active site of the DNA polymerase in a proper polarity
-
physiological function
-
the bacterial primase is an essential component in the replisome, molecular mechanisms at the DNA replication apparatus, overview
-
physiological function
-
the helicase-primase interaction is an essential event in DNA replication and is mediated by the highly variable C-terminal domain (CTD) of primase (DnaG) and N-terminal domain (NTD) of helicase (DnaB)
-
physiological function
-
the bacterial primase is an essential component in the replisome, molecular mechanisms at the DNA replication apparatus, overview
-
physiological function
-
the helicase-primase interaction is an essential event in DNA replication and is mediated by the highly variable C-terminal domain (CTD) of primase (DnaG) and N-terminal domain (NTD) of helicase (DnaB)
-
physiological function
-
DnaG binds to the Csl4 RNA-degrading exosome but not to the Rrp4-exosome of Saccharolobus solfataricus. DnaG is a poly(A)-binding protein enhancing the degradation of adenine-rich transcripts by the Csl4-exosome
-
additional information
comparison of bacterial and archaeal DnaG and composition of reconstituted Sulfolobus solfataricus exosomes, overview
additional information
Mtb DnaG primase homology structure modelling
additional information
structure function relationship of DnaG primase, overview
additional information
structure function relationship of DnaG primase, overview
additional information
structure function relationship of DnaG primase, overview
additional information
structure modeling using the MtDnaG-CTD and MtDnaB-NTD crystal structures for analysis of crucial helicase-primase interaction in Mycobacterium tuberculosis. Two nonconserved hydrophobic residues (Ile605 and Phe615) of MtDnaG are identified as potential key residues interacting with MtDnaB. The loop, connecting the two helices of the HHR, is concluded to be largely responsible for the stability of the DnaB-DnaG complex. Molecular dynamic simulations were performed on the models of the MtDnaB-NTD complex with DnaG-CTD, DnaG-CTD I605A, and DnaG-CTD F615A. Structure comparisons of the enzyme from Mycobacterium tuberculosis with enzymes from other species. Residue Ile605 in the HHR is crucial for helicase-primase interaction. The dimer-dimer interface of MtDnaB-NTD is considered as a DnaG-binding site. Mycobacterium DnaB-NTD interacts with DnaG-CTD of other organisms with low binding affinity
additional information
structure of bacterial primase DnaG in complex with the bacterial replicative helicase DnaB, structure comparisons, overview
additional information
structure of bacterial primase DnaG in complex with the bacterial replicative helicase DnaB, structure comparisons, overview
additional information
the C-terminal hexapeptide motif of SSB (DDDIPF, SSB-Ct) is highly conserved and is known to engage in essential interactions with many proteins in nucleic acid metabolism, including primase. The SSB-Ct binding site in DnaGC has been identified by NMR. The binding pocket is formed by basic residues K447, R452, and K518, as well as T450, M451, I455, and L519. The conserved R452 residue forms a salt bridge with the carboxylic acid of the C-terminal Phe residue of the SSB-Ct, whereas the other positively charged residues around the binding pocket interact with the negatively charged residues of SSB-Ct
additional information
using a replication system containing the origin of replication of the single-stranded DNA phage G4 (G4ori) saturated with SSB, it is tested whether DnaG and pol III can bind concurrently to the primed template. The binding of both proteins to SSB is mutually exclusive. Using a replication system containing the origin of replication of the single-stranded DNA phage G4 (G4ori) saturated with SSB. Both primase and the chi subunit of pol III interact with the highly conserved C-terminus of single-stranded DNA-binding protein (SSB). About 10 nucleotides have to be added in order to displace one of the two primase molecules bound to SSB-saturated G4ori, specific binding of DnaG primase to G4ori. In a ssM13Gori replication system, DNA polymerase III holoenzyme does not displace primase from ssM13Gori. After primer synthesis in the absence of CTP, half of the primase is displaced from ssM13Gori/SSB by an addition of pol III and dTTP, dGTP and dCTP. Only the mixture of dTTP, dGTP and dCTP causes significant primase dissociation: about half of the enzyme is released from the complex
additional information
-
structure function relationship of DnaG primase, overview
-
additional information
-
Mtb DnaG primase homology structure modelling
-
additional information
-
structure function relationship of DnaG primase, overview
-
additional information
-
structure modeling using the MtDnaG-CTD and MtDnaB-NTD crystal structures for analysis of crucial helicase-primase interaction in Mycobacterium tuberculosis. Two nonconserved hydrophobic residues (Ile605 and Phe615) of MtDnaG are identified as potential key residues interacting with MtDnaB. The loop, connecting the two helices of the HHR, is concluded to be largely responsible for the stability of the DnaB-DnaG complex. Molecular dynamic simulations were performed on the models of the MtDnaB-NTD complex with DnaG-CTD, DnaG-CTD I605A, and DnaG-CTD F615A. Structure comparisons of the enzyme from Mycobacterium tuberculosis with enzymes from other species. Residue Ile605 in the HHR is crucial for helicase-primase interaction. The dimer-dimer interface of MtDnaB-NTD is considered as a DnaG-binding site. Mycobacterium DnaB-NTD interacts with DnaG-CTD of other organisms with low binding affinity
-
additional information
-
Mtb DnaG primase homology structure modelling
-
additional information
-
structure function relationship of DnaG primase, overview
-
additional information
-
structure modeling using the MtDnaG-CTD and MtDnaB-NTD crystal structures for analysis of crucial helicase-primase interaction in Mycobacterium tuberculosis. Two nonconserved hydrophobic residues (Ile605 and Phe615) of MtDnaG are identified as potential key residues interacting with MtDnaB. The loop, connecting the two helices of the HHR, is concluded to be largely responsible for the stability of the DnaB-DnaG complex. Molecular dynamic simulations were performed on the models of the MtDnaB-NTD complex with DnaG-CTD, DnaG-CTD I605A, and DnaG-CTD F615A. Structure comparisons of the enzyme from Mycobacterium tuberculosis with enzymes from other species. Residue Ile605 in the HHR is crucial for helicase-primase interaction. The dimer-dimer interface of MtDnaB-NTD is considered as a DnaG-binding site. Mycobacterium DnaB-NTD interacts with DnaG-CTD of other organisms with low binding affinity
-
Show AA Sequence and Transmembrane Helices (40641 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
the C-terminal domain MtDnaG-CTD is a dimer in solution, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
an N-terminal zinc-binding domain (ZBD) responsible for DNA template recognition, a central catalytic domain (RNA polymerase domain, RPD), and a C-terminal helicase-binding domain (HBD or DnaGC), which is responsible for interaction with DnaB helicase and single-stranded DNA-binding protein (SSB)
additional information
DnaG is organized in three domains, the N-terminal zinc-binding domain (ZBD), the central RNA polymerase domain (RPD) and the C-terminal helicase-binding domain (HBD). The role of the ZBD is to recognize the priming site, which is 5'-C(A/T)G. The RPD carries the active site with three catalytic acidic residues that are exposed at a cleft in the center of the protein. This part of the proteins has structural similarity with the toprim fold, a region of about 100 amino acids found in topoisomerases. The HBD anchors the primase at the hexameric ring of the helicase. The latter interaction is particularly important as DnaG is activated about 5000fold when bound to DnaB. Within the replisome, two DnaG molecules cooperate, one molecule binding the template at the trinucleotide priming site and the other catalyzing primer synthesis
additional information
DnaG is organized in three domains, the N-terminal zinc-binding domain (ZBD), the central RNA polymerase domain (RPD) and the C-terminal helicase-binding domain (HBD). The role of the ZBD is to recognize the priming site, which is 5'-C(A/T)G. The RPD carries the active site with three catalytic acidic residues that are exposed at a cleft in the center of the protein. This part of the proteins has structural similarity with the toprim fold, a region of about 100 amino acids found in topoisomerases. The HBD anchors the primase at the hexameric ring of the helicase. The latter interaction is particularly important as DnaG is activated about 5000fold when bound to DnaB. Within the replisome, two DnaG molecules cooperate, one molecule binding the template at the trinucleotide priming site and the other catalyzing primer synthesis
additional information
in a crystal structure of the Geobacillus stearothermophilus DnaB6-(DnaGC)3 complex, the three C-terminal domains of primase each bind to two adjacent subunits of the dilated N-tier of DnaB
additional information
MtDnaG-CTD interacts at the dimer-dimer interface of MtDnaB-NTD using mostly hydrophobic residues of the helical hairpin regions (HHRs). The dimer-dimer interface of MtDnaB-NTD is considered as a DnaG-binding site
additional information
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MtDnaG-CTD interacts at the dimer-dimer interface of MtDnaB-NTD using mostly hydrophobic residues of the helical hairpin regions (HHRs). The dimer-dimer interface of MtDnaB-NTD is considered as a DnaG-binding site
-
additional information
-
MtDnaG-CTD interacts at the dimer-dimer interface of MtDnaB-NTD using mostly hydrophobic residues of the helical hairpin regions (HHRs). The dimer-dimer interface of MtDnaB-NTD is considered as a DnaG-binding site
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additional information
archaeal DnaG contains N- and C-terminal domains flanking a TOPRIM domain. The N-terminal domain is a RNA-binding domain with poly(rA)-preference cooperating with the TOPRIM domain in binding of RNA
additional information
DnaG primase is composed of three functional domains: the N-terminal zinc-binding domain (ZBD) responsible for DNA binding specificity, the RNA polymerase domain (RPD) responsible for enzymatic activity, and the C-terminal domain (CTD) responsible for the interaction with the DnaB helicase. Structure determination and anaysis of the C-terminal domain (CTD), solution structure and dynamics of the DnaG primase CTD, conformations and flexibility, overview. It has two subdomains, the first six helices create the C1 subdomain and the last two helices, alpha7 and alpha8, create the C2 subdomain. The primase CTD is in the closed conformation, but NMR dynamic studies indicate there is considerable movement in the linker between the two subdomains and that N564 is the most dynamic residue within the linker
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of the RNA polymerase domain of DnaG. The tethered zinc binding domain plays an important role in the interactions between primase and specific template sequence. The ssDNA template binding surface is L-shaped, a model for the template ssDNA binding to primase is proposed. Comparison with the enzyme from Geobacillus stearothermophilus
structures of hexameric helicase DnaB and its complex with the helicase binding domain of DnaG. Within the hexamer the two domains of DnaB pack with different symmetries to form a distinct two-layered ring structure. Each of three bound DnaG helicase binding domains stabilizes the DnaB hexamer in a conformation that may increase its processivity. Three positive, conserved electrostatic patches on the N-terminal domain of DnaB may also serve as a binding site for DNA and guide the DNA to a DnaG active site
crystal structures of noncovalent DnaG-DNA complexes, of the RNA polymerase domain of DnaG and various DNA ligands. A key site for DnaG interaction with ds/ss DNA, located on the N-terminal subdomain of the RNAS polymerase domain
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purified recombinant C-terminal domain of DnaG, mixing of 0.002 ml of 6 mg/ml native MtDnaG-CTD and 5 mg/ml selenomethionine-labeled MtDnaG-CTD with 0.002 ml of reservoir solution containing 20% w/v PEG 3350, 0.2 M magnesium acetate tetrahydrate, and equilibration against 0.5 ml of reservoir solution, for the SeMet-labeled protein a reeservoir solution of reservoir solution of 18% w/v PEG 3350, 0.15 M magnesium acetate, and MOPS, pH 7.6, is used, 4°C, 1-2 weeks, X-ray diffraction structure determination and analysis at 1.57-1.58 A resolution, modeling
structures of the DnaG catalytic core bound to metal ion cofactors and either individual nucleoside triphosphates or the nucleotidyl alarmones, pppGpp and ppGpp
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K447A
K478A
mutant shows binding affinities to SSB similar to wild-type DnaG C-terminus
K518A
K528A
mutant shows binding affinities to SSB similar to wild-type DnaG C-terminus
K580A
site-directed mutagenesis, the mutant shows 1.6fold recombineering efficiency compared to wild-type
Q576A
site-directed mutagenesis, the mutant shows 2.8fold recombineering efficiency compared to wild-type
Q576T/K580A
site-directed mutagenesis, the mutant shows 3.6-7.0fold recombineering efficiency compared to wild-type
Q576V/K580A
site-directed mutagenesis, the mutant shows 5.4-7.5fold recombineering efficiency compared to wild-type
R452A
T450A
I605A
site-directed mutagenesis, mutant MtDnaG-CTD I605A, binding study shows a significant decrease in the binding affinity of MtDnaB-NTD with the Ile605Ala mutant of MtDnaG-CTD compared with native MtDnaG-CTD
I605A
-
site-directed mutagenesis, mutant MtDnaG-CTD I605A, binding study shows a significant decrease in the binding affinity of MtDnaB-NTD with the Ile605Ala mutant of MtDnaG-CTD compared with native MtDnaG-CTD
-
I605A
-
site-directed mutagenesis, mutant MtDnaG-CTD I605A, binding study shows a significant decrease in the binding affinity of MtDnaB-NTD with the Ile605Ala mutant of MtDnaG-CTD compared with native MtDnaG-CTD
-
E175Q
additional information
K447A
site-directed mutagenesis, the DnaGC point mutant shows dramatically attenuated SSB-Ct binding
K518A
site-directed mutagenesis, the DnaGC point mutant shows dramatically attenuated SSB-Ct binding
R452A
site-directed mutagenesis, the DnaGC point mutant shows dramatically attenuated SSB-Ct binding
T450A
site-directed mutagenesis, the DnaGC point mutant shows dramatically attenuated SSB-Ct binding
E175Q
mutation drastically reduces priming activity, low level of DNA binding activity
E175Q
site-directed mutagenesis of the TOPRIM domain, DnaGE175Q has a poly(rA) preference like wild-type DnaG
additional information
ssDNA recombineering and CRISPR-Cas9 are combined for the generation of DnaG variants. The tightly regulated Red operon expression cassette and tightly regulated Cas9 expression cassette are integrated into one chloroamphenicol resistance, p15A replicon-based vector. A self-curing, kanamycin resistance, p15A replicon-based plasmid is applied for the plasmid elimination after genome editing. The genome editing efficiency is as high as 100%. The recombineering efficiency of the strains harboring the DnaG variants is assayed via the kanamycin resistance gene repair as well as the chromosomal gene deletion experiments. Genotype analysis. THe Q576A/K580A double variant cannot be generated, Q576A/K580A is lethal to Escherichia coli
additional information
-
ssDNA recombineering and CRISPR-Cas9 are combined for the generation of DnaG variants. The tightly regulated Red operon expression cassette and tightly regulated Cas9 expression cassette are integrated into one chloroamphenicol resistance, p15A replicon-based vector. A self-curing, kanamycin resistance, p15A replicon-based plasmid is applied for the plasmid elimination after genome editing. The genome editing efficiency is as high as 100%. The recombineering efficiency of the strains harboring the DnaG variants is assayed via the kanamycin resistance gene repair as well as the chromosomal gene deletion experiments. Genotype analysis. THe Q576A/K580A double variant cannot be generated, Q576A/K580A is lethal to Escherichia coli
additional information
a fusion protein consisting of the full-length Csl4 and the N-terminal domain of enzyme DnaG catalyzes the degradation of A-rich RNA by the exosome. Construction of a His-tagged enzyme mutant lacking the N-terminal domain, analysis of interaction between the Csl4 exosome and His6-DnaG-DELTANT
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from insoluble recombinant aggregates, solubilization by addition of high concentrations of glycerol, polyethylene glycol, or Mn2+, and by incubation at 60°C
overproduced recombinant polypeptide is insoluble, aggregates can be dissolved in the presence of 3 M urea
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recombinant His-tagged -type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
recombinant His-tagged DnaG from Escherichia coli by nickel affinity chromatography, co-purification of Strep-tagged Csl4 and His-tagged Rrp4, Rrp41, Rrp42 and DnaG
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli, copurification of the His6-tagged wild-type enzyme with His6-tagged Rrp4, Csl4, Rrp41 and Rrp42, and Strep-tagged Csl4
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene dnaG, recombinant expression of His-tagged wild-type and mutant enzymes, and of unlabeled and selenomethionine-labeled MtDnaG-CTDs in Escherichia coli strain BL21(DE3)
gene dnaG, sequence comparisons, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli, coexpression with His6-tagged Rrp4, Csl4, Rrp41 and Rrp42, and Strep-tagged Csl4
recombinant expression of central and C-terminal domains of Escherichia coli DnaG primase (residues 111-581), here called DnaG-RCD, and of amino acid residues 115-581
recombinant expression of His-tagged DnaG in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
low expression level, stable folding of the dnaG mRNA may significantly contribute to this
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
drug development
the bacterial primase is a target for antibiotic drugs, inhibitors of DNA primase provide antibiotic agents. Bacterial replisome as a multiple-drug target
drug development
the bacterial primase is a target for antibiotic drugs, inhibitors of DNA primase provide antibiotic agents. Bacterial replisome as a multiple-drug target
drug development
the bacterial primase is a target for antibiotic drugs, inhibitors of DNA primase provide antibiotic agents. Bacterial replisome as a multiple-drug target
drug development
the DnaG-DnaB interaction is an attractive antibiotic target because it is conserved in bacteria, essential for DNA replication, and is distinctly different from that of viruses, archaea, and eukaryotes
drug development
-
the bacterial primase is a target for antibiotic drugs, inhibitors of DNA primase provide antibiotic agents. Bacterial replisome as a multiple-drug target
-
drug development
-
the bacterial primase is a target for antibiotic drugs, inhibitors of DNA primase provide antibiotic agents. Bacterial replisome as a multiple-drug target
-
drug development
-
the bacterial primase is a target for antibiotic drugs, inhibitors of DNA primase provide antibiotic agents. Bacterial replisome as a multiple-drug target
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zuo, Z.; Rodgers, C.J.; Mikheikin, A.L.;, Trakselis, M.A.
Characterization of a functional DnaG-type primase in archaea: implications for a dual-primase system
J. Mol. Biol.
397
664-676
2010
Saccharolobus solfataricus (P95980), Saccharolobus solfataricus
brenda
Hou, L.; Klug, G.; Evguenieva-Hackenberg, E.
Archaeal DnaG contains a conserved N-terminal RNA-binding domain and enables tailing of rRNA by the exosome
Nucleic Acids Res.
42
12691-12706
2014
Saccharolobus solfataricus (P95980)
brenda
Hou, L.; Klug, G.; Evguenieva-Hackenberg, E.
The archaeal DnaG protein needs Csl4 for binding to the exosome and enhances its interaction with adenine-rich RNAs
RNA Biol.
10
415-424
2013
Saccharolobus solfataricus (P95980)
brenda
Hou, C.; Biswas, T.; Tsodikov, O.V.
Structures of the catalytic domain of bacterial primase DnaG in complexes with DNA provide insight into key priming events
Biochemistry
57
2084-2093
2018
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
brenda
Szafranski, P.; Smith, C.L.; Cantor, C.R.
Cloning and analysis of the dnaG gene encoding Pseudomonas putida DNA primase
Biochim. Biophys. Acta
1352
243-248
1997
Pseudomonas putida (P0A119)
brenda
Ayora, S.; Langer, U.; Alonso, J.
Bacillus subtilis DnaG primase stabilises the bacteriophage SPP1 G40P helicase-ssDNA complex
FEBS Lett.
439
59-62
1998
Bacillus subtilis
-
brenda
Fouser, L.; Bird, R.
Accumulation of ColE1 early replicative intermediates catalyzed by extracts of Escherichia coli dnaG mutant strains
J. Bacteriol.
154
1174-1183
1983
Escherichia coli (P0ABS5)
brenda
Thirlway, J.; Soultanas, P.
In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues
J. Bacteriol.
188
1534-1539
2006
Geobacillus stearothermophilus (Q9X4D0)
brenda
Reichard, P.; Rowen, L.; Eliasson, R.; Hobbs, J.; Eckstein, F.
Inhibition of primase, the dnaG protein of Escherichia coli by 2-deoxy-2-azidocytidine triphosphate
J. Biol. Chem.
253
7011-7016
1978
Escherichia coli (P0ABS5)
brenda
Rowen, L.; Kornberg, A.
Primase, the dnaG protein of Escherichia coli. An enzyme which starts DNA chains
J. Biol. Chem.
253
758-764
1978
Escherichia coli (P0ABS5)
brenda
Sims, J.; Capon, D.; Dressler, D.
dnaG (primase)-dependent origins of DNA replication. Nucleotide sequences of the negative strand initiation sites of bacteriophages St-1, phiK, and alpha3
J. Biol. Chem.
254
12615-12628
1979
Escherichia coli
brenda
Benz Jr., E.; Reinberg, D.; Vicuna, R.; Hurwitz, J.
Initiation of DNA replication by the dnaG protein
J. Biol. Chem.
255
1096-1106
1980
Escherichia coli
brenda
Gardiennet, C.; Wiegand, T.; Bazin, A.; Cadalbert, R.; Kunert, B.; Lacabanne, D.; Gutsche, I.; Terradot, L.; Meier, B.; Bckmann, A.
Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori
J. Biomol. NMR
64
189-195
2016
Helicobacter pylori (P56064), Helicobacter pylori ATCC 700392 (P56064)
-
brenda
Zuo, Z.; Rodgers, C.J.; Mikheikin, A.L.; Trakselis, M.A.
Characterization of a functional DnaG-type primase in archaea implications for a dual-primase system
J. Mol. Biol.
397
664-676
2010
Saccharolobus solfataricus (P95980), Saccharolobus solfataricus, Saccharolobus solfataricus ATCC 35092 (P95980)
brenda
Ilyina, T.; Gorbalenya, A.; Koonin, E.
Organization and evolution of bacterial and bacteriophage primase-helicase systems
J. Mol. Evol.
34
351-357
1992
Escherichia coli
brenda
Aravind, L.; Leipe, D.D.; Koonin, E.V.
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Geobacillus stearothermophilus (Q9X4D0)
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The helicase-binding domain of Escherichia coli DnaG primase interacts with the highly conserved C-terminal region of single-stranded DNA-binding protein
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Escherichia coli (P0ABS5)
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Rannou, O.; Le Chatelier, E.; Larson, M.A.; Nouri, H.; Dalmais, B.; Laughton, C.; Janniere, L.; Soultanas, P.
Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis
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Bacillus subtilis (P05096), Bacillus subtilis, Bacillus subtilis 168 (P05096)
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The archaeal DnaG protein needs Csl4 for binding to the exosome and enhances its interaction with adenine-rich RNAs
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Saccharolobus solfataricus (P95980), Saccharolobus solfataricus DSM 1617 (P95980)
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Bailey, S.; Eliason, W.; Steitz, T.
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Rymer, R.; Solorio, F.; Tehranchi, A.; Chu, C.; Corn, J.; Keck, J.; Wang, J.; Berger, J.
Binding mechanism of metal-NTP substrates and stringent-response alarmones to bacterial DnaG-type primases
Structure
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Staphylococcus aureus (O05338), Escherichia coli (P0ABS5)
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Lilien, C.
Escherichia coli dnaG gene product is required for a normal rate of phage T4 DNA synthesis
Virology
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Escherichia coli
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Hakeem, S.; Singh, I.; Sharma, P.; Verma, V.; Chandra, R.
In silico screening and molecular dynamics simulations study to identify novel potent inhibitors against Mycobacterium tuberculosis DnaG primase
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Mycobacterium tuberculosis (P9WNW1), Mycobacterium tuberculosis ATCC 25618 (P9WNW1), Mycobacterium tuberculosis H37Rv (P9WNW1)
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Chilingaryan, Z.; Headey, S.J.; Lo, A.T.Y.; Xu, Z.Q.; Otting, G.; Dixon, N.E.; Scanlon, M.J.; Oakley, A.J.
Fragment-based discovery of inhibitors of the bacterial DnaG-SSB interaction
Antibiotics
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Escherichia coli (P0ABS5)
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Ilic, S.; Cohen, S.; Singh, M.; Tam, B.; Dayan, A.; Akabayov, B.
DnaG primase-A target for the development of novel antibacterial agents
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Bacillus subtilis (P05096), Bacillus subtilis 168 (P05096), Escherichia coli (P0ABS5), Mycobacterium tuberculosis (P9WNW1), Mycobacterium tuberculosis ATCC 25618 (P9WNW1), Mycobacterium tuberculosis H37Rv (P9WNW1)
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Li, J.; Sun, J.; Gao, X.; Wu, Z.; Shang, G.
Coupling ssDNA recombineering with CRISPR-Cas9 for Escherichia coli DnaG mutations
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Escherichia coli (P0ABS5), Escherichia coli
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Sharma, D.P.; Vijayan, R.; Rehman, S.A.A.; Gourinath, S.
Structural insights into the interaction of helicase and primase in Mycobacterium tuberculosis
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Mycobacterium tuberculosis (P9WNW1), Mycobacterium tuberculosis ATCC 25618 (P9WNW1), Mycobacterium tuberculosis H37Rv (P9WNW1)
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Catazaro, J.; Periago, J.; Shortridge, M.D.; Worley, B.; Kirchner, A.; Powers, R.; Griep, M.A.
Identification of a ligand-binding site on the Staphylococcus aureus DnaG primase C-terminal domain
Biochemistry
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Staphylococcus aureus (O05338)
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Bergsch, J.; Allain, F.H.; Lipps, G.
Recent advances in understanding bacterial and archaeoeukaryotic primases
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Escherichia coli (P0ABS5), Geobacillus stearothermophilus (Q9X4D0)
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Monachino, E.; Jergic, S.; Lewis, J.S.; Xu, Z.Q.; Lo, A.T.Y.; O'Shea, V.L.; Berger, J.M.; Dixon, N.E.; van Oijen, A.M.
A primase-induced conformational switch controls the stability of the bacterial replisome
Mol. Cell
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140-154.e7
2020
Escherichia coli (P0ABS5), Geobacillus stearothermophilus (Q9X4D0)
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Bogutzki, A.; Naue, N.; Litz, L.; Pich, A.; Curth, U.
E. coli primase and DNA polymerase III holoenzyme are able to bind concurrently to a primed template during DNA replication
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14460
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Escherichia coli (P0ABS5)
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