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Information on EC 3.1.31.1 - micrococcal nuclease
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3.1.31.1 micrococcal nucleaseSpecify your search results
Word Map
- 3.1.31.1
- chromatin
- nucleosomes
- histone
- nuclei
- strand
- nucleases
-
mononucleosomes
- dnaase
- deoxyribonuclease
-
footprint
- coagulase
- nucleoprotein
- enterotoxin
-
nonhistone
-
oligonucleosomes
-
octamer
- ribonucleoprotein
- polycephalum
-
chromatin-associated
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non-transcribed
- medicine
-
protein-dna
- globin
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staphylococci
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native-like
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internucleosomal
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hyperacetylated
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snrnp
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telomeres
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nuclease-resistant
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32p-postlabeling
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decondensation
- physarum
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minichromosome
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chromatin-bound
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endonucleolytic
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coagulase-positive
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coagulase-negative
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end-labeling
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histone-dna
- beta-globin
- drug development
- molecular biology
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superhelical
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supercoiled
-
exonuclease
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dielectric
- analysis
-
i-hypersensitive
-
ladder
-
base-pairs
- biotechnology
- cscl
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heterochromatic
-
nucleolytic
The enzyme appears in viruses and cellular organisms
Reaction Schemes
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
Synonyms
micrococcal nuclease, staphylococcal nuclease, mnase, snase, thermonuclease, tudor-sn, staphylococcus aureus nuclease, tudor staphylococcal nuclease, staphylococcal nuclease a, s. aureus nuclease, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.1.4.7
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-
formerly
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micrococcal DNase
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-
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micrococcal endonuclease
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-
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Micrococcal nuclease
MN
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-
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MNase
Nuc
NUC1
Nuc2
nuclease 8V
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nuclease T
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-
-
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nuclease T'
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nuclease, micrococcal
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-
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nuclease, staphylococcal
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NucM
ribonucleate (deoxyribo-nucleate) 3'-nucleotidohydrolase
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ribonucleate (deoxyribonucleate) 3'-nucleotidohydrolase
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S. aureus nuclease
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SNA
snake venom phosphodiesterase
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SNase
SNAseR
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analogue of SNAse A EC 3.1.4.7, in which hexapeptide is appended to the alanine of SNAse A
SND1
spleen endonuclease
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spleen phosphodiesterase
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staph nuclease
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-
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staphylococcal nuclease
Staphylococcal nuclease A
staphylococcus aureus nuclease
staphylococcus aureus nuclease B
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thermonuclease
TNase
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TSN
tudor staphylococcal nuclease
Micrococcal nuclease
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SNase
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SNase
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SNase
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staphylococcal nuclease
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staphylococcal nuclease
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staphylococcal nuclease
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staphylococcus aureus nuclease
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staphylococcus aureus nuclease
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Nuc, named NucB when secreted as an active 168-amino acid-long polypeptide
thermonuclease
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
mechanism
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
mechanism
-
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
mechanism
-
-
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
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-
-
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CAS REGISTRY NUMBER
COMMENTARY
9013-53-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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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-
?
ss-DNA + H2O
?
single strand salmon sperm DNA, obtained by boiling for 30 min and rapid cooling on ice
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-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
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-
-
-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
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+ oligonucleotides terminated by 3'-phosphate, produced only in incomplete digestion
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
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in native DNA Xp-dTp and Xp-dAp bonds are preferentially attached in denaturated DNA random cleavage
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-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
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denaturated DNA is hydrolyzed more rapidly than native DNA
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-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
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in native DNA Xp-dTp and Xp-dAp bonds are preferentially attached in denaturated DNA random cleavage
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-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
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denaturated DNA is hydrolyzed more rapidly than native DNA
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-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
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in native DNA Xp-dTp and Xp-dAp bonds are preferentially attached in denaturated DNA random cleavage
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-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
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denaturated DNA is hydrolyzed more rapidly than native DNA
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-
?
DNA + H2O
3'-deoxymononucleotides + dinucleotides
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?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
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dinucleotides terminated by 3'-phosphates
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
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nucleoside 3'-phosphates of both purines and pyrimidines
?
RNA + H2O
nucleoside 3'-phosphates + dinucleotides
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-
-
?
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
?
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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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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
?
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GFP-dsDNA and GFP-dsRNA are not used as substrates
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?
additional information
?
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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
?
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enzyme does not cleave the 2',3'-cyclic phosphate derivates of the ribonucleosides
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-
?
additional information
?
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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
?
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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
?
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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
?
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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
?
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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
?
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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
-
-
?
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
?
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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'
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-
?
additional information
?
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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
?
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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
?
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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
?
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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'
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-
?
additional information
?
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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
?
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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
?
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-
substrate is single-strand salmon sperm DNA
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
the enzyme possesses calcium-dependent nuclease activity specific to ssRNA, but not dsRNA and DNA
-
-
?
additional information
?
-
-
the enzyme possesses calcium-dependent nuclease activity specific to ssRNA, but not dsRNA and DNA
-
-
?
additional information
?
-
-
essential enzyme in the life cycle of Plasmodium falciparum
-
-
?
additional information
?
-
-
staphylococcal nuclease R, an analogue of the enzyme has the same activity and structural feature as the wild type enzyme
-
-
?
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
-
-
?
additional information
?
-
-
micrococcal nuclease induces double-strand breaks within nucleosome linker regions, and with more extensive digestion, single-strand nicks within the nucleosome itself
-
-
?
additional information
?
-
-
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
additional information
Ca2+
activates to 120% of initial activity at 0.05 mM
Ca2+
-
hydrolysis of DNA and RNA is completely dependent on Ca2+, KM for wild-type enzyme is 0.113 mM
Ca2+
-
1 mM, unfolding forces in the presence of calcium ion are slightly increased
Ca2+
-
the carboxylic groups in the active site of SNase are known to bind Ca2+
additional information
the enzyme activity is not affected by Mg2+ and Mn2+
additional information
-
the enzyme activity is not affected by Mg2+ and Mn2+
additional information
isozyme Nuc1 only exhibits a very small increase in thermonuclease activity in the presence of Ca2+ (0.05 mM), Mg2+ (0.05 mM), Co2+ (0.5 mM) and Ni2+ (0.05 mM)
additional information
isozyme Nuc1 only exhibits a very small increase in thermonuclease activity in the presence of Ca2+ (0.05 mM), Mg2+ (0.05 mM), Co2+ (0.5 mM) and Ni2+ (0.05 mM)
additional information
-
isozyme Nuc1 only exhibits a very small increase in thermonuclease activity in the presence of Ca2+ (0.05 mM), Mg2+ (0.05 mM), Co2+ (0.5 mM) and Ni2+ (0.05 mM)
additional information
isozyme Nuc2 activity is cation-dependent
additional information
isozyme Nuc2 activity is cation-dependent
additional information
-
examination of salt sensitivity of pka-values (chemical shifts analyzed by NMR while titrating) His8, His46, His121 and His124. Tested variants D21N/T33V/T41I/S59A/P117G/A128A mutant, E75A mutant, E75Q mutant, and E101A mutant in 0.01 M, 0.10 M, and 1.0 M KCl
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2'-deoxythymidine 3',5'-diphosphate
-
at 100 microM concentration of pdTp, parasites show block in development, most of the parasites appear dead or shrunken within six hours after inhibitor treatment
3',5'-deoxythymidine diphosphate
-
addition to the cell culture medium blocks further growth
adenosine 3',5'-diphosphate
-
able to induce folding of mutant proteins into the native state
caspase-3
Tudor staphylococcal nuclease, a multifunctional regulator of gene expression, is cleaved by caspase-3 during apoptosis, this cleavage impairs the ability of Tudor staphylococcal nuclease to activate mRNA splicing, inhibits its ribonuclease activity and is important for the execution of apoptosis, cleavage of enzyme lowers its nuclease activity by almost 50%
-
Co2+
isozyme Nuc1 shows 79% activity at 5 mM concentration
deoxythymidine 3',5'-diphosphate
-
in the presence of pdTp, unfolding forces increase drastically
Mn2+
isozyme Nuc1 activity drops sharply at 5 mM concentration; isozyme Nuc2 activity decreases with an increase in Mn2+ concentration
deoxythymidine 3',5'-bisphosphate
nuclease activity of enzyme is highly sensitive to deoxythymidine 3',5'-bisphosphate, a specific inhibitor of staphylococcal nuclease, whereas the inactive analogue deoxythymidine 3'-phosphate has no inhibitory effect
deoxythymidine 3',5'-bisphosphate
nuclease activity of PaTSN is highly sensitive to deoxythymidine 3',5'-bisphosphate, a specific inhibitor of staphylococcal nuclease, whereas the inactive analogue deoxythymidine 3'-phosphate has no inhibitory effect
metacaspase mcII-Pa
metacaspase mcII-Pa cleaves the phylogenetically conserved protein Tudor staphylococcal nuclease during both developmental and stress-induced programmed cell death
-
metacaspase mcII-Pa
metacaspase mcII-Pa processes recombinant enzyme into 5 major fragments, inactivation of mcII-Pa either by the inhibitor EGR-chloromethyl ketone or through mutation of catalytic Cys139 blocked Tudor staphylococcal nuclease fragmentation, proteolysis of endogenous enzyme correlates with metacaspase activity, reaching the maximum level in early embryos and declining to non-detectable levels in mature embryos, cleavage of enzyme by mcII-Pa leads to a 90% decrease in ribonuclease activity, whereas inactivation of mcII-Pa by either EGR-cmk or mutation of catalytic Cys139 left TSN intact and fully active
-
Zn2+
isozyme Nuc1 activity drops sharply at 5 mM concentration; isozyme Nuc2 activity decreases with an increase in Zn2+ concentration
additional information
induction of apoptosis in HCT116 colon carcinoma cells with 5-fluorouracil leads to increased caspase-3-like activity and cleavage of endogenous Tudor staphylococcal nuclease into 2 fragments with the same molecular mass in vitro, this effect is not cell- and drug-specific because a similar pattern of endogenous Tudor staphylococcal nuclease cleavage is detected in camptothecin-treated HeLa cells
-
additional information
-
induction of apoptosis in HCT116 colon carcinoma cells with 5-fluorouracil leads to increased caspase-3-like activity and cleavage of endogenous Tudor staphylococcal nuclease into 2 fragments with the same molecular mass in vitro, this effect is not cell- and drug-specific because a similar pattern of endogenous Tudor staphylococcal nuclease cleavage is detected in camptothecin-treated HeLa cells
-
additional information
Nuc2 shows weaker activity, lower thermostability and different sensitivity to Zn2+ and Mn2+, and in the presence of EDTA or SDS compared with Nuc1, which is consistent with differences in the sequence pattern and structure predicted; Nuc2 shows weaker activity, lower thermostability and different sensitivity to Zn2+ and Mn2+, and in the presence of EDTA or SDS compared with Nuc1, which is consistent with differences in the sequence pattern and structure predicted
-
additional information
Nuc2 shows weaker activity, lower thermostability and different sensitivity to Zn2+ and Mn2+, and in the presence of EDTA or SDS compared with Nuc1, which is consistent with differences in the sequence pattern and structure predicted; Nuc2 shows weaker activity, lower thermostability and different sensitivity to Zn2+ and Mn2+, and in the presence of EDTA or SDS compared with Nuc1, which is consistent with differences in the sequence pattern and structure predicted
-
additional information
-
Nuc2 shows weaker activity, lower thermostability and different sensitivity to Zn2+ and Mn2+, and in the presence of EDTA or SDS compared with Nuc1, which is consistent with differences in the sequence pattern and structure predicted; Nuc2 shows weaker activity, lower thermostability and different sensitivity to Zn2+ and Mn2+, and in the presence of EDTA or SDS compared with Nuc1, which is consistent with differences in the sequence pattern and structure predicted
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE