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3'-O-acetylnitrophenyl-pdT + H2O
?
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?
5'-chloromethyl-pdTp-nitrophenyl + H2O
?
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?
5'-O-acetyl-dTp-nitrophenyl + H2O
?
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-
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?
5'-sulfate-dTp-nitrophenyl + H2O
?
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-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
dTp-nitrophenyl + H2O
?
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-
-
-
?
GFP-ssDNA + H2O
?
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-
partial degradation
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?
GFP-ssRNA + H2O
?
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-
complete degradation
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?
M13mp18 DNA + H2O
?
-
circular single stranded DNA
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-
?
methyl-pdTp-nitrophenyl + H2O
?
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-
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-
?
nitrophenyl-pdTp + H2O
?
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-
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?
nitrophenyl-pdTpdTp-nitrophenyl + H2O
?
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-
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-
?
RNA + H2O
?
the enzyme cleaves RNA chains at the 5'-side of the phosphodiester linkage to produce degraded fragments with 5'-hydroxyl and 3'-phosphate ends. cTSN degrades single-stranded RNA and double-stranded RNA containing mismatched base pairs, but is not restricted to those containing multiple I/U and U/I pairs. Tudor staphylococcal nuclease is a structure-specific ribonuclease targeting single-stranded RNA and unstructured regions of double-stranded RNA
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-
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
ss-DNA + H2O
?
single strand salmon sperm DNA, obtained by boiling for 30 min and rapid cooling on ice
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-
?
ssDNA + H2O
?
-
single stranded salmon sperm DNA
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-
?
additional information
?
-
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
-
-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
-
-
-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
-
+ oligonucleotides terminated by 3'-phosphate, produced only in incomplete digestion
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
in native DNA Xp-dTp and Xp-dAp bonds are preferentially attached in denaturated DNA random cleavage
-
-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
denaturated DNA is hydrolyzed more rapidly than native DNA
-
-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
in native DNA Xp-dTp and Xp-dAp bonds are preferentially attached in denaturated DNA random cleavage
-
-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
denaturated DNA is hydrolyzed more rapidly than native DNA
-
-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
-
-
-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
-
-
-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
in native DNA Xp-dTp and Xp-dAp bonds are preferentially attached in denaturated DNA random cleavage
-
-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
denaturated DNA is hydrolyzed more rapidly than native DNA
-
-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
-
-
-
-
?
nitrophenyl-pdT + H2O
?
-
-
-
-
?
nitrophenyl-pdT + H2O
?
-
-
-
-
?
nitrophenyl-pdT + H2O
?
-
-
-
-
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
-
-
-
-
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
-
-
-
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
-
-
-
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
-
-
-
-
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
-
-
dinucleotides terminated by 3'-phosphates
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
-
-
nucleoside 3'-phosphates of both purines and pyrimidines
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
-
-
-
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
-
-
-
-
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
-
-
-
?
additional information
?
-
the enzyme possesses calcium-dependent nuclease activity specific to ssRNA, but not dsRNA and DNA
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-
?
additional information
?
-
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the enzyme possesses calcium-dependent nuclease activity specific to ssRNA, but not dsRNA and DNA
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-
?
additional information
?
-
substrates are double-stranded RNA targeting PAZ domain of PmAgo1, PmRab7, and gfp. The enzyme shows calcium-dependent RNase activity, overview
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-
?
additional information
?
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-
substrates are double-stranded RNA targeting PAZ domain of PmAgo1, PmRab7, and gfp. The enzyme shows calcium-dependent RNase activity, overview
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-
?
additional information
?
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essential enzyme in the life cycle of Plasmodium falciparum
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-
?
additional information
?
-
-
GFP-dsDNA and GFP-dsRNA are not used as substrates
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-
?
additional information
?
-
-
-
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-
?
additional information
?
-
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specificity
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-
?
additional information
?
-
-
inhibition when a 5'-phosphomonoester end group is present in an oligonucleotide
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-
?
additional information
?
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-
best substrates oligonucleotides with a 3'-phosphomonoester end group
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-
?
additional information
?
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substrate masking: binding of RNA by EGTA-inactivated enzyme results in artifactual inhibition of RNA processing
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-
?
additional information
?
-
-
enzyme does not cleave the 2',3'-cyclic phosphate derivates of the ribonucleosides
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-
?
additional information
?
-
-
staphylococcal nuclease R, an analogue of the enzyme has the same activity and structural feature as the wild type enzyme
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-
?
additional information
?
-
-
poly-his-nuclease R can be used both for removal of contaminated DNA and RNA and for separating the enzyme from target proteins
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-
?
additional information
?
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micrococcal nuclease induces double-strand breaks within nucleosome linker regions, and with more extensive digestion, single-strand nicks within the nucleosome itself
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-
?
additional information
?
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the enzyme cuts nucleosomal DNA asymmetrically, predominantly in the A/T sequences closest to the nucleosome core/linker junctions. The extent of chromatosomal DNA protected by histone H1 depends on the nucleotide sequence in the linker DNA, overview
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-
?
additional information
?
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enzyme detection based on peptide-bridged energy transfer between mercaptoacetic acid capped CdSe/ZnS quantum dots and dye-labeled ROX-modified 20-mer single-stranded DNA containing AT-rich regions, overview
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-
?
additional information
?
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isozyme Nuc1 is active with genomic DNA extracted from Staphylococcus aureus, Listeria monocytogenes, and Salmonella, herring sperm DNA, plasmid DNA pNucc from Staphylococcus aureus and pBR122 from Escherichia coli, and RNA from Staphylococcus aureus, substrate specificity of the recombinant nuclease, overview
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-
?
additional information
?
-
isozyme Nuc1 is active with genomic DNA extracted from Staphylococcus aureus, Listeria monocytogenes, and Salmonella, herring sperm DNA, plasmid DNA pNucc from Staphylococcus aureus and pBR122 from Escherichia coli, and RNA from Staphylococcus aureus, substrate specificity of the recombinant nuclease, overview
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-
?
additional information
?
-
-
isozyme Nuc1 is active with genomic DNA extracted from Staphylococcus aureus, Listeria monocytogenes, and Salmonella, herring sperm DNA, plasmid DNA pNucc from Staphylococcus aureus and pBR122 from Escherichia coli, and RNA from Staphylococcus aureus, substrate specificity of the recombinant nuclease, overview
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-
?
additional information
?
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isozyme Nuc2 is active with genomic DNA extracted from Staphylococcus aureus, Listeria monocytogenes, and Salmonella, herring sperm DNA, plasmid DNA pNucc from Staphylococcus aureus and pBR122 from Escherichia coli, and RNA from Staphylococcus aureus, substrate specificity of the recombinant nuclease, overview
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-
?
additional information
?
-
isozyme Nuc2 is active with genomic DNA extracted from Staphylococcus aureus, Listeria monocytogenes, and Salmonella, herring sperm DNA, plasmid DNA pNucc from Staphylococcus aureus and pBR122 from Escherichia coli, and RNA from Staphylococcus aureus, substrate specificity of the recombinant nuclease, overview
-
-
?
additional information
?
-
-
isozyme Nuc2 is active with genomic DNA extracted from Staphylococcus aureus, Listeria monocytogenes, and Salmonella, herring sperm DNA, plasmid DNA pNucc from Staphylococcus aureus and pBR122 from Escherichia coli, and RNA from Staphylococcus aureus, substrate specificity of the recombinant nuclease, overview
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-
?
additional information
?
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label-free and sensitive detection of micrococcal nuclease activity using DNA-scaffolded silver nanoclusters as a fluorescence indicator, evaluation of the quantitative method, overview. The ssDNA is introduced as the enzyme substrate and also as the scaffold for the synthesis of the silver nanoclusters. Since the ssDNA probe P3 acts not only as the substrate for MNase, but also as the scaffold for the silver nanoclusters, the concentration of P3 is obviously a critical factor for the MNase assay. With an increase in P3 concentration, the fluorescence intensity increases either in the presence or absence of the enzyme
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-
?
additional information
?
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method development for an ultra-high sensitive and selective fluorescent sensing platform for the enzyme based on enzyme-induced DNA strand scission and the difference in affinity of graphene oxide for single-stranded DNA containing different numbers of bases in length, overview. The adsorption of the dye-labeled ssDNA on graphene oxide makes the dyes close proximity to graphene oxide surface resulting in high efficiency quenching of fluorescence of the dyes. Conversely, and very importantly, in the presence of MNase, it cleaves the dye-labeled ssDNA into small fragments. Substrates are commercial and 6-carboxyfluorescein (FAM)-labeled: 20-mer ssDNA with a sequence of 5'-FAM-TATATGGATGATGTGGTATT-3', 10-mer ssDNA with a sequence of 5'FAM-TATATGGATG-3', and 5-mer ssDNA with a sequence of 5'FAM-TATAT-3'
-
-
?
additional information
?
-
-
nucleosomal DNA sizes varying between 147 and 155 bp, the positions of the MNase cuts reflect positions of the A-T pairs rather than the nucleosome core/linker junctions. But a combined treatment with the enzyme and exonuclease III overcomes the enzyme's sequence preference producing nucleosomal DNA trimmed symmetrically and precisely at the core/linker junctions regardless of the underlying DNA sequence, overview. Digestion of the nucleosomes containing CATG tetranucleotide at different positions in relation to the core/linker DNA junction
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-
?
additional information
?
-
substrates are chicken and recombinant frog chromatins, as well as mixture of two plasmid DNAs, one harbouring a 10841-bp segment of sheep DNA containing the beta-lactoglobulin gene and the other harbouring a 13626-bp segment of Saccharomyces cerevisiae DNA incorporating a late-firing replication yeast replication origin, reconstituted with limiting amounts of core histones by salt gradient dialysis. Chromatins, prepared by reconstitution with either chicken or frog histones, are digested to mononucleosomes using micrococcal nuclease, identification of the locations and quantification of the strength of both the chicken or frog histone octamer binding sites on each DNA, the enzyme shows sequence specificity in its preferred cleavage sites with a preference to cut at sites centred on A/T-containing dinucleotides, and comparison to the activity of caspase-activated DNase, overview
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-
?
additional information
?
-
the wild-type and truncated mutant isozyme Nuc2 degrades several nucleotide substrates, including Staphylococcus aureus genomic DNA, eukaryotic salmon sperm DNA, double-stranded plasmid DNA, and single-stranded DNA
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-
?
additional information
?
-
the wild-type and truncated mutant isozyme Nuc2 degrades several nucleotide substrates, including Staphylococcus aureus genomic DNA, eukaryotic salmon sperm DNA, double-stranded plasmid DNA, and single-stranded DNA
-
-
?
additional information
?
-
-
method development for an ultra-high sensitive and selective fluorescent sensing platform for the enzyme based on enzyme-induced DNA strand scission and the difference in affinity of graphene oxide for single-stranded DNA containing different numbers of bases in length, overview. The adsorption of the dye-labeled ssDNA on graphene oxide makes the dyes close proximity to graphene oxide surface resulting in high efficiency quenching of fluorescence of the dyes. Conversely, and very importantly, in the presence of MNase, it cleaves the dye-labeled ssDNA into small fragments. Substrates are commercial and 6-carboxyfluorescein (FAM)-labeled: 20-mer ssDNA with a sequence of 5'-FAM-TATATGGATGATGTGGTATT-3', 10-mer ssDNA with a sequence of 5'FAM-TATATGGATG-3', and 5-mer ssDNA with a sequence of 5'FAM-TATAT-3'
-
-
?
additional information
?
-
-
specificity
-
-
?
additional information
?
-
the wild-type and truncated mutant isozyme Nuc2 degrades several nucleotide substrates, including Staphylococcus aureus genomic DNA, eukaryotic salmon sperm DNA, double-stranded plasmid DNA, and single-stranded DNA
-
-
?
additional information
?
-
the wild-type and truncated mutant isozyme Nuc2 degrades several nucleotide substrates, including Staphylococcus aureus genomic DNA, eukaryotic salmon sperm DNA, double-stranded plasmid DNA, and single-stranded DNA
-
-
?
additional information
?
-
isozyme Nuc1 is active with genomic DNA extracted from Staphylococcus aureus, Listeria monocytogenes, and Salmonella, herring sperm DNA, plasmid DNA pNucc from Staphylococcus aureus and pBR122 from Escherichia coli, and RNA from Staphylococcus aureus, substrate specificity of the recombinant nuclease, overview
-
-
?
additional information
?
-
-
specificity
-
-
?
additional information
?
-
-
substrate is single-strand salmon sperm DNA
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-
?
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evolution
sequence comparison and phylogenetic analysis, Staphylococcus clustering, overview. The divergent Staphylococcus aureus clade harbors a homologue of the thermostable nuclease (NucM) whose nucleotide sequence is highly divergent from those of nuc1 and nuc2 of Staphylococcus aureus reference strains
evolution
-
sequence comparison and phylogenetic analysis, Staphylococcus clustering, overview. The divergent Staphylococcus aureus clade harbors a homologue of the thermostable nuclease (NucM) whose nucleotide sequence is highly divergent from those of nuc1 and nuc2 of Staphylococcus aureus reference strains
-
evolution
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sequence comparison and phylogenetic analysis, Staphylococcus clustering, overview. The divergent Staphylococcus aureus clade harbors a homologue of the thermostable nuclease (NucM) whose nucleotide sequence is highly divergent from those of nuc1 and nuc2 of Staphylococcus aureus reference strains
-
evolution
-
sequence comparison and phylogenetic analysis, Staphylococcus clustering, overview. The divergent Staphylococcus aureus clade harbors a homologue of the thermostable nuclease (NucM) whose nucleotide sequence is highly divergent from those of nuc1 and nuc2 of Staphylococcus aureus reference strains
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malfunction
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when the nuc1 gene is knocked out, the ability of Staphylococcus aureus strains to form a biofilm significantly increased
malfunction
-
conditioned medium from Hep3B-SND1 cells stably overexpressing SND1 augmentes, whereas that from QGYSND1si cells stably overexpressing SND1 siRNA significantly inhibits angiogenesis, as analyzed by a chicken chorioallantoic membrane assay and a human umbilical vein endothelial cell differentiation assay
malfunction
mutations of either or both of the nuclease genes nuc1 and nuc2 result in an enhanced capacity to form a biofilm, mutation of nuc2 also has an impact on the ability of a sarA mutant to form a biofilm, at least in the absence of coating with plasma proteins. The susceptibility to daptomycin is reduced in the mutants
malfunction
mutations of either or both of the nuclease genes nuc1 and nuc2 result in an enhanced capacity to form a biofilm. The susceptibility to daptomycin is reduced in the mutants
malfunction
suppression of Penaeus monodon Tudor staphylococcal nuclease by double-stranded RNA results in decreasing dsRNA-mediated gene silencing activity. Knockdown of Argonaute protein PmAgo1 and the enzyme diminishes the ability of dsRNA-Rab7 to knockdown PmRab7 expression
malfunction
-
mutations of either or both of the nuclease genes nuc1 and nuc2 result in an enhanced capacity to form a biofilm. The susceptibility to daptomycin is reduced in the mutants
-
malfunction
-
when the nuc1 gene is knocked out, the ability of Staphylococcus aureus strains to form a biofilm significantly increased
-
metabolism
programmed cell death pathways, Tudor staphylococcal nuclease is a new component of the human programmed degradome and is cleaved by caspase-3 between the Tudor and SN5 domains
metabolism
programmed cell death, enzyme is a part of the stress-induced cell-death degradome during both developmental and stress-induced cell deaths
metabolism
extracellular DNA promotes biofilm formation in Staphylococcus aureus and, conversely, extracellular nucleases limit the ability to form a biofilm
metabolism
-
inhibition of NF-kappaB blocks enzyme-induced angiogenesis
metabolism
-
extracellular DNA promotes biofilm formation in Staphylococcus aureus and, conversely, extracellular nucleases limit the ability to form a biofilm
-
physiological function
ribonuclease activity, control of gene expression by activating transcription, subsequent mRNA splicing, regulation of RNA silencing and in the pathway that edits and destroys double-stranded RNA, uncleavable Tudor staphylococcal nuclease stimulates cell proliferation and protects cells from death
physiological function
-
Staphylococcal nuclease degrades both DNA and RNA
physiological function
staphylococcal nuclease domain-containing protein 1 is a component of the RNA-induced splicing complex that mediates RNA interference, leading to degradation of specific mRNAs
physiological function
-
presence and ionization of Lys66, buried in the hydrophobic core of a stabilized variant of staphylococcal nuclease, affect conformation and dynamics. The neutral Lys66 affects slow conformational fluctuations globally, whereas the effects of the charged form are localized to the region immediately surrounding position 66, when Lys66 is charged the protein expands, structural reorganization triggered by ionization of the internal Lys66, detailed overview
physiological function
-
staphylococcal nuclease is an important virulence factor of Staphylococcus aureus. Biofilm development can be prevented in staphylococcal nuclease-producing strains of Staphylococcus aureus, direct relationship between staphylococcal nuclease production and the prevention of biofilm development, overview. Staphylococcal nuclease affects biofilm formation by other bacteria, such as Pseudomonas aeruginosa and Staphylococcus epidermis. Only bacterial strains that do not possess the nuc1 gene are able to form biofilms
physiological function
-
Staphylococcus aureus nuclease mediates resistance against entrapment and killing within neutrophil extracellular traps, which consist of a nuclear DNA backbone associated with antimicrobial peptides, histones and proteases that provide a matrix to entrap and kill various microbes. Promoting role of Staphylococcus aureus nuclease in neutrophil extracellular traps degradation and virulence in a murine respiratory tract infection model, overview. Staphylococcus aureus nuclease facilitates evasion from neutrophil extracellular trap entrapment, and mediates resistance against extracellular killing by neutrophils
physiological function
-
enzyme hepatocellular carcinoma Staphylococcal nuclease domain containing-1 promotes tumorigenesis in human hepatocellular carcinoma cells. It increases angiotensin II type 1 receptor (AT1R) levels by increasing AT1R mRNA stability. That results in activation of ERK, Smad2 and subsequently the TGFbeta signaling pathway, promoting epithelial-mesenchymal transition and migration and invasion by human hepatocellular carcinoma cells. The enzyme modulates the TGFbeta signaling pathway
physiological function
extracellular nucleases limit the ability to form a biofilm. The role of extracellular nucleases under in vitro versus in vivo conditions differ
physiological function
involvement of PmAgo1 and the enzyme in shrimp RNAi pathway, RNAi-based mechanism in shrimp, overview
physiological function
isozyme Nuc2 is detrimental to Staphylococcus aureus biofilms, purified isozyme Nuc2 prevents biofilm formation in vitro and modestly decreases biomass in dispersal experiments
physiological function
major role for isozyme Nuc1 in terms of thermonuclease activity
physiological function
-
the enzyme is a stress-related protein, enzyme Tudor-SN plays an important role in the assembly of AGTR1-3' UTR granules affecting the recovery kinetics of stress granules
physiological function
-
the enzyme staphylococcal nuclease domain-containing 1, SND1, regulates a variety of cellular functions and promotes an aggressive tumorigenic phenotype in hepatocellular carcinoma cells. Role of SND1 in regulating tumor angiogenesis, a hallmark of cancer, overview. SND1 regulates NF-kappaB and miR-221, two important determinants of hepatocellular carcinoma controlling the aggressive phenotype. The enzyme induces angiogenesis by up-regulating angiogenin and CXCL16. The phosphorylation of IKKalpha and IkappaBalpha upon enzyme overexpression suggests activation of a canonical NF-kappa B signaling pathway by the enzyme
physiological function
-
the MNase digestion of nucleosomes assembled on a strong nucleosome positioning sequence, Widom's clone 601, releases nucleosome cores whose sizes are strongly affected by the linker DNA sequence
physiological function
-
the nuc gene necoding Staphylococcus aureus nuclease is under the control of the SaeRS two-component system, which is a major regulator of Staphylococcus aureus virulence determinants, the enzyme is an SaeRS-dependent virulence factor. With community-associated methicillin-resistant Staphylococcus aureus in a mouse model of peritonitis, in vivo expression of Nuc activity in an SaeRS-dependent manner is observed and determination of Nuc as a virulence factor that is important for in vivo survival, confirming the enzyme's role as a contributor to invasive disease. The enzyme contributes to pathogen survival during invasive disease
physiological function
the downregulated expression of Tudor-staphylococcal nuclease can decrease cancer malignancy, and the overexpression can increase viability and migration potential of various tumor cell types. Tudor-SN silencing suppresses the expression of alkylglycerone phosphate synthase (AGPS) and the activity of the mechanistic target of rapamycin (mTOR) signaling pathway. NF-kappaB and miR-127 may be the mediators of Tudor-SN-regulated alkylglycerone phosphate synthase (AGPS) via the mTOR signaling pathway
physiological function
the enzyme cooperates with RNA editing to eliminate duplex RNA in cell defense. Tudor staphylococcal nuclease selects and degrades RNA during microRNA decay
physiological function
-
isozyme Nuc2 is detrimental to Staphylococcus aureus biofilms, purified isozyme Nuc2 prevents biofilm formation in vitro and modestly decreases biomass in dispersal experiments
-
physiological function
-
extracellular nucleases limit the ability to form a biofilm. The role of extracellular nucleases under in vitro versus in vivo conditions differ
-
physiological function
-
major role for isozyme Nuc1 in terms of thermonuclease activity
-
physiological function
-
Staphylococcus aureus nuclease mediates resistance against entrapment and killing within neutrophil extracellular traps, which consist of a nuclear DNA backbone associated with antimicrobial peptides, histones and proteases that provide a matrix to entrap and kill various microbes. Promoting role of Staphylococcus aureus nuclease in neutrophil extracellular traps degradation and virulence in a murine respiratory tract infection model, overview. Staphylococcus aureus nuclease facilitates evasion from neutrophil extracellular trap entrapment, and mediates resistance against extracellular killing by neutrophils
-
physiological function
-
staphylococcal nuclease is an important virulence factor of Staphylococcus aureus. Biofilm development can be prevented in staphylococcal nuclease-producing strains of Staphylococcus aureus, direct relationship between staphylococcal nuclease production and the prevention of biofilm development, overview. Staphylococcal nuclease affects biofilm formation by other bacteria, such as Pseudomonas aeruginosa and Staphylococcus epidermis. Only bacterial strains that do not possess the nuc1 gene are able to form biofilms
-
additional information
-
MNase mapping of the enhancer chromatin structure in the Drosophila melanogaster embryo to analyse chromatin structure in a developmental setting, and identification of structural changes on a cis-regulatory element targeted by the Knirps repressor, method development and optimization, overview
additional information
-
residue W140 is critical to SNase structure and function
additional information
-
thermodynamic parameters derived from urea-induced unfolding of mutant SNase140 and mutant SNase141 in comparison with those of wild-type SNase and mutant SNase140 in the presence of calcium, backbone dynamics, detailed overview. Mutant SNase140 unfolds easily compared to mutant SNase141 and wild-type SNase
additional information
-
enzyme tryptophan fluorescence spectra, fluorescence measurements of protein unfolding under pressure, high-pressure fluorescence spectroscopy and single value decomposition analysis, overview
additional information
-
mannosylglycerate preferentially affects specific structural elements of the P117G/H124L/S128A mutant enzyme, structure analysis, overview
additional information
sequence and structure comparisons of isozymes Nuc1 and Nuc2, overview
additional information
sequence and structure comparisons of isozymes Nuc1 and Nuc2, overview
additional information
-
staphylococcal nuclease domain-containing 1, SND1, is a multifunctional nuclease containing four staphylococcal nuclease domains and a tudor domain. No potential interaction between enzyme SND1 and p65 subunit of NF-kappa B
additional information
the enzyme interacts with Argonaute protein PmAgo1, but not with PmAgo2 or PmAgo3. Interaction between PmAgo and the enzyme is mediated through the N-terminal domain of PmAgo1 and the SN1-2 domains of the enzyme, interaction analysis and mapping using the two-hybrid system for different protein constructs, overview
additional information
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the enzyme interacts with Argonaute protein PmAgo1, but not with PmAgo2 or PmAgo3. Interaction between PmAgo and the enzyme is mediated through the N-terminal domain of PmAgo1 and the SN1-2 domains of the enzyme, interaction analysis and mapping using the two-hybrid system for different protein constructs, overview
additional information
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the fluorescence detected guanidine hydrochloride equilibrium denaturation of wild-type staphylococcal nuclease does not fit a three-state unfolding model, overview. Method evaluation to distinguish a two-state from a three-state denaturation
additional information
-
the introduction of internal cavities into different subdomains affects local stability, flexibility, and dynamics of the enzyme, NMR spectroscopy under atmospheric and high pressure, H/D exchange and molecular dynamics simulations of wild-type and mutant enzymes, overview. Responses to the creation of cavities cannot be anticipated from global thermodynamic stability or crystal structures, they depend on the local structural and energetic context of the substitutions
additional information
-
sequence and structure comparisons of isozymes Nuc1 and Nuc2, overview
-
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D790E
by site-directed mutagenesis, proteolysis of Tudor staphylococcal nuclease does not occur either when the P1 position of the DAVD motif is mutated or after treatment with the pan-caspase inhibitor zVAD-fluoromethylketone, expression of mutant under normal conditions enhances cell proliferation in both cancer (HeLa) and non-cancer (HEK-293) cells compared with mock- and wild-type Tudor staphylococcal nuclease-transfected samples, under camptothecin-induced apoptosis, expression of Tudor staphylococcal nuclease mutant results in a 35% increment in viable HeLa cells, suggesting that caspase-mediated proteolysis of enzyme is important for the progression of apoptosis
DELTA140-149
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deletion of the 10 C-terminal residues, mutant proteins are in a non-native or disordered state under physiological conditions, folding is induced by addition of an inhibitor or substrate
F34A
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site-directed mutagenesis
G79S/H124LC80-C116
-
effects on the stability and conformation of the folded protein
H124LC77-C118
-
effects on the stability and conformation of the folded protein
H124LC79-C118
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effects on the stability and conformation of the folded protein
H124LC80-C116
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effects on the stability and conformation of the folded protein
I92A
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site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme
INS33A34
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insertion of an alanine between residues 33 and 34, mutant proteins are in a non-native or disordered state under physiological conditions, folding is induced by addition of an inhibitor or substrate
K45C
-
insertion of a cysteine to enable labeling with thiol reactive ligands, e.g. 5,5'-dithiobis-2-nitrobenzoic acid, CD-spectra of wild type enzyme, mutant and mutant with 5,5'-dithiobis-2-nitrobenzoic acid label indicate, that the protein have very similar secondary structures
L103A
-
site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme
L125A
-
site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme
L25A
-
site-directed mutagenesis
L36A
-
site-directed mutagenesis
L38A
-
site-directed mutagenesis
P117G,/H124L/S128A
-
site-directed mutagenesis, a highly stable triple mutant
P117G/H124L/S128A
-
site-directed mutagenesis
P11A/P31A/P42A/P47T/P56A/P117G
proline free mutant, conformationally different from wild type protein, 1.4% of wild type activity
P47G/P117G/H124L/W140H
-
tryptophan-free mutant used for the insertion of a unique tryptophan at positions 15, 27, 61, 76, 91, 102, and 121, mutant enzymes used to study the enzyme folding kinetics, variants are destabilized but maintain the ability to refold in the native-like structure
T62C
-
designed for the insertion of a cysteine reactive label
T62P
highly destabilized variant of enzyme, exists in the unfolded state over a wide pH-range, can be fully refolded to the native folding by addition of osmolytes
V23A
-
site-directed mutagenesis
V66A
-
site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme
V66F/P117G,/H124L/S128A
-
site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared
V66G/P117G,/H124L/S128A
-
site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared
V66N/P117G,/H124L/S128A
-
site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared
V66Q/P117G,/H124L/S128A
-
site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared
V66S/P117G,/H124L/S128A
-
site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared
V66T/P117G,/H124L/S128A
-
site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared
V66Y/P117G,/H124L/S128A
-
site-directed mutagenesis of the highly stable triple mutant P117G,/H124L/S128A, thermodynamic stability during guanidine hydrochloride denaturation of mutants is compared
V74A
-
site-directed mutagenesis
A128S
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to study inductive effects and longer-range interactions between elements of the network, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy)
A1C/Q149C
-
SNase double mutant, N- and C-terminal residues replaced by cysteine, constructed from the plasmid (pMT7-SN) of wild-type SNase using the Kunkel method, can form disulfide bond
A90S
-
pH-value, at which the acid-denaturation is half completed is 4.19, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.0 for the mutant enzyme compared to 1.8 for wild-type enzyme
D143G
-
Tm value for mutant enzyme is 50.53°C, compared to 50.98°C for wild-type enzyme
D146G
-
Tm value for mutant enzyme is 50.99°C, compared to 50.98°C for wild-type enzyme
D19G
-
Tm value for mutant enzyme is 52.06°C, compared to 50.98°C for wild-type enzyme
D21G
-
Tm value for mutant enzyme is 53.74°C, compared to 50.98°C for wild-type enzyme
D21N/T33V/T41I/S59A/P117G/A128A
-
hyperstable engineered form of staphylococcal nuclease (SNase)
D40G
-
Tm value for mutant enzyme is 50.44°C, compared to 50.98°C for wild-type enzyme
D77A
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to study inductive effects and longer-range interactions between elements of the network, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy) , determination of tautomeric states of His121 and His124, pH near pI
D83G
-
Tm value for mutant enzyme is 37.21°C, compared to 50.98°C for wild-type enzyme
D95G
-
Tm value for mutant enzyme is 37.38°C, compared to 50.98°C for wild-type enzyme
DELTA1-139
-
mutant lacks tertiary structure, fluorescence of the mutant is much lower than that of the wild-type enzyme
DELTA1-141
-
intact tertiary conformation, melting point is nearly identical to wild-type enzyme
E101A
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to examine shortrange effects on His124, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy)
E101G
-
Tm value for mutant enzyme is 43.04°C, compared to 50.98°C for wild-type enzyme
E10G
-
Tm value for mutant enzyme is 43.8°C, compared to 50.98°C for wild-type enzyme
E122G
-
Tm value for mutant enzyme is 44.12°C, compared to 50.98°C for wild-type enzyme
E129G
-
Tm value for mutant enzyme is 34.59°C, compared to 50.98°C for wild-type enzyme
E135G
-
Tm value for mutant enzyme is 44.54°C, compared to 50.98°C for wild-type enzyme
E135Q
-
charge neutralization
E142G
-
Tm value for mutant enzyme is 49.41°C, compared to 50.98°C for wild-type enzyme
E43G
-
Tm value for mutant enzyme is 54.99°C, compared to 50.98°C for wild-type enzyme
E52G
-
Tm value for mutant enzyme is 52.1°C, compared to 50.98°C for wild-type enzyme
E57G
-
Tm value for mutant enzyme is 46.6°C, compared to 50.98°C for wild-type enzyme
E67G
-
Tm value for mutant enzyme is 46.53°C, compared to 50.98°C for wild-type enzyme
E73A
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to study inductive effects and longer-range interactions between elements of the network, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy)
E73G/D77G
-
loss of thermal stabilty of 47% relative to the wild-type protein
E73G/E75G
-
loss of thermal stabilty of 59% relative to the wild-type protein
E73G/E75G/D77G
-
loss of thermal stabilty of 65% relative to the wild-type protein
E75A
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to examine short-range (up to 6.4 Angstrom) Coulomb and hydrogen bonding effects on His121, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy), determination of tautomeric states of His121 and His124, pH near pI
E75G
-
Tm value for mutant enzyme is 36.99°C, compared to 50.98°C for wild-type enzyme
E75G/D77G
-
loss of thermal stabilty of 58% relative to the wild-type protein
F34W/W140F
-
characterized by far and near UV CD, gel filtration, ANS-binding fluorescence, enzymatic parameters are similar to those of the wild type, similar substrate affinity to the wild type enzyme
F61W/W140A
-
the mutant shows reduced activity with higher Michaelis-Menten constants, Km, and lower maximum reaction rate compared to the wild-type enzyme, the mutant also shows a more rapid loss of secondary and tertiary structure by Gdn-HCl unfolding than the wild-type enzyme
F76W/W140H
-
mutation causes decrease in thermal stability
G20A
-
2% of wild-type activity. Km(Ca) is almost 20fold higher than the wild-type enzyme. Denaturation midpoint for the mutant enzyme is 1.5 M urea compared to 2.0 M urea for the wild-type enzyme
G20I
-
0.21% of wild-type activity. Km(Ca) is almost 50fold higher than the wild-type enzyme. Denaturation midpoint for mutant enzyme is 0.82 M urea compared to 2.0 M urea for the wild-type enzyme
G20V
-
0.45% of wild-type activity. Km(Ca) is almost 20fold higher than the wild-type enzyme. Denaturation midpoint for the mutynt enzyme is 1.1 M urea compared to 2.0 M urea for the wild-type enzyme
G50F/V51N/P117G/H124L/S128A/DELTA44-49
-
hyperstable, acid-resistant mutant form of enzyme known as delta+PHS
G79S
-
pH-value, at which the acid-denaturation is half completed is 4.39, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.4 for the mutant enzyme compared to 1.8 for wild-type enzyme
G88V
-
pH-value, at which the acid-denaturation is half completed is 3.57, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 3.0 for the mutant enzyme compared to 1.8 for wild-type enzyme
H124L
-
pH-value, at which the acid-denaturation is half completed is 2.98, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 2.8 for the mutant enzyme compared to 1.8 for wild-type enzyme
H124Q
-
charge neutralization
I92E
-
wild-type enzyme exhibits a broad range of pH-independence from pH 4.5 to pH 9, mutant enzyme exhibits pronounced pH-dependence with a maximal stability at pH 4.9
I92K
-
wild-type enzyme exhibits a broad range of pH-independence from pH 4.5 to pH 9.0, mutant enzyme exhibits pronounced pH-dependence with a maximal stability at pH 9.8
K127A
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to examine shortrange effects on His124, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy)
K127Q
-
charge neutralization
K133A
-
intact tertiary conformation, melting point is 4.6°C lower than that of the wild-type enzyme
K133Q
-
charge neutralization
K28C/H124C
-
generated by site-directed mutagenesis, native and non-native conformations are observed, and the non-native conformation expands with increasing guanidinium hydrochloride concentrations, the non-native chains of the derivative exhibits different changes of persistence length at higher guanidinium hydrochloride concentrations, suggesting a subdomain-specific collapse of the denatured state of SNase, this local chain specific collapse is likely to play a role in modulating the formation of early intermediate during protein folding
K28C/K97C
-
generated by site-directed mutagenesis, native and non-native conformations are observed, and the non-native conformation expands with increasing guanidinium hydrochloride concentrations, the non-native chains of the derivative exhibits different changes of persistence length at higher guanidinium hydrochloride concentrations, suggesting a subdomain-specific collapse of the denatured state of SNase, this local chain specific collapse is likely to play a role in modulating the formation of early intermediate during protein folding
K28Q
-
charge neutralization
K48Q
-
charge neutralization
K63Q
-
charge neutralization
K64Q
-
charge neutralization
K70Q
-
charge neutralization
K78Q
-
charge neutralization
K84Q
-
charge neutralization
K97Q
-
charge neutralization
K9A
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to study inductive effects and longer-range interactions between elements of the network, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy)
L25A
-
pH-value, at which the acid-denaturation is half completed is 4.15, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.2 for the mutant enzyme compared to 1.8 for wild-type enzyme
S28C
-
this mutant contains a five-amino acid type I beta-turn from concanavalin A in place of residues 27-30 of SNase
V66D/P117G/H124L/S128A
-
production by site-directed mutagenesis, pka value shifts to 7.79 and, after chemical denaturation, to 8.05
V66D/P117G/H124L/S128A/G50F/V51N/DELTA44-49
-
production by site-directed mutagenesis, pka value shifts to 8.95 and, after chemical denaturation, to 8.73
V66E/P117G/H124L/S128A
-
production by site-directed mutagenesis, pka value shifts to 8.80 and, after chemical denaturation, to 8.99
V66E/P117G/H124L/S128A/G50F/V51N/DELTA44-49
-
production by site-directed mutagenesis, pka value shifts to 9.07 and, after chemical denaturation, to 8.80
V66K/P117G/H124L/S128A
-
production by site-directed mutagenesis, pka value shifts to 6.35
V66K/P117G/H124L/S128A/G50F/V51N/DELTA44-49
-
production by site-directed mutagenesis, pka value shifts to 5.63 and, after chemical denaturation, to 5.83
V66L
-
pH-value, at which the acid-denaturation is half completed is 3.36, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 2.6 for the mutant enzyme compared to 1.8 for wild-type enzyme
V66L/G79S/G88V
-
pH-value, at which the acid-denaturation is half completed is 3.67, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.1 for the mutant enzyme compared to 1.8 for wild-type enzyme
V66L/G88V
-
pH-value, at which the acid-denaturation is half completed is 3.42, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.6 for the mutant enzyme compared to 1.8 for wild-type enzyme
W140C
-
DNA hydrolysis activity is 75% of wild-type activity
W140D
-
DNA hydrolysis activity is 65% of wild-type activity
W140E
-
DNA hydrolysis activity is 65% of wild-type activity
W140G
-
DNA hydrolysis activity is 75% of wild-type activity
W140I
-
DNA hydrolysis activity is 70% of wild-type activity
W140K
-
DNA hydrolysis activity is 70% of wild-type activity
W140M
-
DNA hydrolysis activity is 70% of wild-type activity
W140N
-
DNA hydrolysis activity is 75% of wild-type activity
W140P
-
DNA hydrolysis activity is 55% of wild-type activity
W140Q
-
DNA hydrolysis activity is 75% of wild-type activity
W140R
-
DNA hydrolysis activity is 75% of wild-type activity
W140S
-
DNA hydrolysis activity is 75% of wild-type activity
W140T
-
DNA hydrolysis activity is 75% of wild-type activity
W140V
-
DNA hydrolysis activity is 75% of wild-type activity
Y54C/I139C
-
production by site-directed mutagenesis, the oxidized form assumes a more compact denatured structure under acidic conditions than the wild type, the kinetic measurements reveal that the refolding reactions of both the reduced and oxidized forms of mutant are similar to those of the wild type protein
Y54C/I139C/DELTA140-149
-
production by site-directed mutagenesis, under physiological conditions, the reduced form appears to assume a denatured structure, in contrast, the oxidized form forms a native-like structure
Y91A
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to examine short-range (up to 6.4 Angstrom) Coulomb and hydrogen bonding effects on His121, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy)
Y91F
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to examine short-range (up to 6.4 Angstrom) Coulomb and hydrogen bonding effects on His121, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy) , determination of tautomeric states of His121 and His124, pH near pI
Y93A
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to examine short-range (up to 6.4 Angstrom) Coulomb and hydrogen bonding effects on His121, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy) , determination of tautomeric states of His121 and His124, pH near pI
Y93F
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to examine short-range (up to 6.4 Angstrom) Coulomb and hydrogen bonding effects on His121, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy) , determination of tautomeric states of His121 and His124, pH near pI
Y93W/W140A
-
the mutant shows reduced activity with higher Michaelis-Menten constants, Km, and lower maximum reaction rate compared to the wild-type enzyme, the mutant also shows a more rapid loss of secondary and tertiary structure by Gdn-HCl unfolding than the wild-type enzyme
D77G
-
loss of catalytic efficiency of 16% and thermal stabilty of 26% relative to the wild-type protein
D77G
-
Tm value for mutant enzyme is 44.14°C, compared to 50.98°C for wild-type enzyme
D77N
-
charge reversal
D77N
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to study inductive effects and longer-range interactions between elements of the network, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy) , determination of tautomeric states of His121 and His124, pH near pI
E73G
-
loss of catalytic efficiency of 24% and thermal stabilty of 22% relative to the wild-type protein
E73G
-
Tm value for mutant enzyme is 37°C, compared to 50.98°C for wild-type enzyme
E75Q
-
charge reversal
E75Q
-
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to examine short-range (up to 6.4 Angstrom) Coulomb and hydrogen bonding effects on His121, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy)
V66K
-
production by site-directed mutagenesis, pka value shifts to 6.38 after chemical denaturation
V66K
-
the substitution affects the H/D exchange properties of the protein globally, even when Lys66 is neutral. The conformational dynamics of the protein probed by H/D exchange indicate that, while both the global fluctuation and the local fluctuation are increased by the substitution, the global fluctuations are enhanced by protonation of Lys-66
W140A
-
DNA hydrolysis activity is 70% of wild-type activity
W140A
-
mutant lacks tertiary structure, fluorescence of the mutant is much lower than that of the wild-type enzyme
W140A
-
the mutant shows reduced activity with higher Michaelis-Menten constants, Km, and lower maximum reaction rate compared to the wild-type enzyme, the mutant also shows a more rapid loss of secondary and tertiary structure by Gdn-HCl unfolding than the wild-type enzyme
W140F
-
mutation causes decrease in thermal stability
W140F
-
native-like structure and native-like activity under physiological conditions
W140H
-
mutation causes decrease in thermal stability
W140H
-
native-like structure and native-like activity under physiological conditions
W140L
-
DNA hydrolysis activity is 75% of wild-type activity
W140L
-
mutation causes decrease in thermal stability
W140Y
-
mutation causes decrease in thermal stability
W140Y
-
native-like structure and native-like activity under physiological conditions
additional information
-
enzyme inactivation by siRNA expression in enzyme-expressing HeLa cells
additional information
-
knockdown of SND1 in QGY-7703 cells inhibits establishment of xenografts in nude mice
additional information
-
suppression in QGY-7703 cells by si RNA, SND1-17-AT1Rsi
additional information
knockdown of the enzyme by dsRNA
additional information
-
knockdown of the enzyme by dsRNA
additional information
construction of nuc1 and nuc1/nuc2 deletion mutant strains
additional information
construction of nuc1 and nuc1/nuc2 deletion mutant strains
additional information
four chimeric His-tagged fusion proteins are constructed by splicing together: 1. the N-terminal Nuc secretion signal or NucB leader to the Nuc2 C-terminal active domain, or 2. the N-terminal Nuc2 membrane anchor to the NucA and NucB C-terminal active domains, construction of nuc2 and nuc1/nuc2 deletion mutant strains
additional information
four chimeric His-tagged fusion proteins are constructed by splicing together: 1. the N-terminal Nuc secretion signal or NucB leader to the Nuc2 C-terminal active domain, or 2. the N-terminal Nuc2 membrane anchor to the NucA and NucB C-terminal active domains, construction of nuc2 and nuc1/nuc2 deletion mutant strains
additional information
generation of a nuc1/nuc2 double deletion mutant
additional information
generation of a nuc1/nuc2 double deletion mutant
additional information
-
generation of a nuc1/nuc2 double deletion mutant
additional information
-
generation of six single mutations were made in a highly stable triple mutant of nucleasemost nuclease, the mutants do not denature by a three-state mechanism, modeling, overview
additional information
-
ten cavity-containing variants of the highly stable form of the enzyme known as DELTA+PHS SNase are described, the DELTA+ PHS reference protein bears stabilizing substitutions in the C-terminal helix (G50F, V51N, P117G, H124L, and S128A), and a deletion of the mobile X loop (residues 44-49), which is part of the active site. Variants with substitutions in the C-terminal domain and the interface between alpha and beta subdomains showed large amide chemical shift variations relative to the parent protein, moderate, widespread, and compensatory perturbations of the H/D protection factors and increased local dynamics on a nanosecond time scale. In contrast, cavity creation in the beta-barrel subdomain leads to minimal perturbation of the structure of the folded state
additional information
-
the enzyme is fused in a chimeric protein to artificial zinc-finger protein, which inhibits virus DNA replication in planta and in 293H cells by blocking binding of a viral replication protein to its replication origin. The resulting hybrid nuclease AZP-SNase cleaves its target DNA plasmid efficiently and sequence-specifically in vitro, and expressed in cells, it inhibits human papillomavirus HPV-18 DNA replication cleaving an HPV-18 ori plasmid around its binding site, overview
additional information
-
four chimeric His-tagged fusion proteins are constructed by splicing together: 1. the N-terminal Nuc secretion signal or NucB leader to the Nuc2 C-terminal active domain, or 2. the N-terminal Nuc2 membrane anchor to the NucA and NucB C-terminal active domains, construction of nuc2 and nuc1/nuc2 deletion mutant strains
-
additional information
-
construction of nuc1 and nuc1/nuc2 deletion mutant strains
-
additional information
-
generation of a nuc1/nuc2 double deletion mutant
-
additional information
-
almost all mutations are destabilizing, the average loss of stability for all of the charge neutralization substitutions is 0.5 kcal/mol and the average loss of stability for all of the charge reversal substitutions is 1.0 kcal/mol
additional information
-
generation by site-directed mutagenesis of C-terminal truncated SNases, i.e. SNase137, SNase139, SNase140, and SNase141 containing residues 1-137, 1-139, 1-140, and 1-141, respectively. The mutants show reduced activities compared to the wild-type enzyme. Determination of the secondary structures of the four SNase fragments, overview
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Alexander, M.; Heppel, L.A.; Hurwitz, J.
The purification and properties of micrococcal nuclease
J. Biol. Chem.
236
3014-3019
1961
Staphylococcus aureus
brenda
Reddi, K.K.
Micrococcal nuclease
Methods Enzymol.
12
257-262
1967
Staphylococcus aureus
-
brenda
Sulkowski, E.; Laskowski, M.
Phosphatase-free crystalline micrococcal nuclease
J. Biol. Chem.
241
4386-4388
1966
Staphylococcus aureus, Staphylococcus aureus Foggi Worthington
brenda
Taniuchi, H.; Anfinsen, C.B.
The amino acid sequence of an extracellular nuclease of Staphylococcus aureus
J. Biol. Chem.
241
4366-4385
1966
Staphylococcus aureus, Staphylococcus aureus V8
brenda
Cotton, F.A.; Hazen, E.E.
Staphylococcal nuclease x-ray structure
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
153-175
1971
Staphylococcus aureus
-
brenda
Anfinsen, C.B; Cuatrecasas, P.; Taniuchi, H.
Staphylococcal nuclease chemical properties and catalysis
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
177-204
1971
Staphylococcus aureus, Staphylococcus aureus V8, Staphylococcus aureus Foggi Worthington
-
brenda
Okabayashi, K.; Mizuno, D.
Surface-bound nuclease of Staphylococcus aureus: localization of the enzyme
J. Bacteriol.
117
215-221
1974
Staphylococcus aureus, Staphylococcus aureus 209P
brenda
Wilchek, M.; Gorecki, M.
Purification of nucleases
Methods Enzymol.
34
492-496
1974
Staphylococcus aureus
brenda
Guisan, J.M.; Ballesteros, A.
Hydrolysis of nucleic acids by sepharose-micrococcal endonuclease
Enzyme Microb. Technol.
3
313-320
1981
Staphylococcus aureus
-
brenda
Cozzone, P.J.; Kaptein, R.
Staphylococcal nuclease and its complexes with nucleotidic inhibitors. A Foto-CIDNP study of aromatic residues exposure
FEBS Lett.
155
55-60
1983
Staphylococcus aureus
-
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