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Literature summary for 3.1.26.4 extracted from

  • Tannous, E.; Kanaya, E.; Kanaya, S.
    Role of RNase H1 in DNA repair removal of single ribonucleotide misincorporated into DNA in collaboration with RNase H2 (2015), Sci. Rep., 5, 9969 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.4

Cloned(Commentary)

Cloned (Comment) Organism
gene rnhA, recombinant overexpression of RNase H1 in Escherichia coli strain MIC3009 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ Mn2+ or Mg2+ are required for catalytic activity Escherichia coli
Mn2+ Mn2+ or Mg2+ are required for catalytic activity Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli ribonuclease H (RNase H) is an endoribonuclease that specifically cleaves the RNA strand of RNA/DNA hybrids1. It cleaves the PO-3' bond of the substrate with a two-metal-ion catalysis mechanism, in which two divalent cations, such as Mg2+ and Mn2+, directly participate in the catalytic function ?
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Organism

Organism UniProt Comment Textmining
Escherichia coli P0A7Y4
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant RNase H1 from Escherichia coli strain MIC3009 to homogeneity Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ribonuclease H (RNase H) is an endoribonuclease that specifically cleaves the RNA strand of RNA/DNA hybrids1. It cleaves the PO-3' bond of the substrate with a two-metal-ion catalysis mechanism, in which two divalent cations, such as Mg2+ and Mn2+, directly participate in the catalytic function Escherichia coli ?
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 ?
additional information cleavage of R9-D9*/D18, R2-D9*/D18, R1-D9*/D18, *D8-R1-D9/D18, D8-R1-D9*/D18, and *D18/D18 duplexes substrates by Escherichia coli RNase H1. Escherichia coli RNase H1 cleaves an Okazaki fragment-like substrate most effectively at R(-2)-R(-1) and less effectively at the RNA-DNA junction in the presence of 5 mM MnCl2, indicating that the RNase H1 exhibits a weak 3'-JRNase activity for this substrate in the presence of manganese ions Escherichia coli ?
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 ?

Synonyms

Synonyms Comment Organism
RNase H1
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 Escherichia coli
rnhA
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 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
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 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 assay at Escherichia coli

General Information

General Information Comment Organism
malfunction disruption of the rnhA gene has been reported to increase a basal level of SOS expression in Escherichia coli, probably due to persistence of R-loops on the chromosome Escherichia coli
physiological function ribonuclease H (RNase H) is an endoribonuclease that specifically cleaves the RNA strand of RNA/DNA hybrids1. It cleaves the PO-3' bond of the substrate with a two-metal-ion catalysis mechanism, in which two divalent cations, such as Mg2+ and Mn2+, directly participate in the catalytic function. Escherichia coli RNase H1 exhibits 3'-JRNase activity for dsDNAR1 much more effectively in the presence of manganese ions than in the presence of magnesium ions, regardless of whether this substrate is cleaved by 5'-JRNase activity of Escherichia coli RNase H2 in advance or not, and can excise the single ribonucleotide in collaboration with Escherichia coli RNase H2. Not only RNase H2 but also RNase H1 is involved in the RER pathway. Role of RNase H1 in DNA repair: removal of single ribonucleotide misincorporated into DNA in collaboration with RNase H2. The 3'-JRNase activity of Escherichia coli RNase H1 may not be involved in SOS response, because this activity may not be required for R-loop resolution Escherichia coli