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Information on EC 3.1.31.1 - micrococcal nuclease and Organism(s) Staphylococcus aureus and UniProt Accession P00644
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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
-
non-transcribed
- medicine
-
protein-dna
- globin
-
staphylococci
-
native-like
-
internucleosomal
-
hyperacetylated
-
snrnp
-
telomeres
-
nuclease-resistant
-
32p-postlabeling
-
decondensation
- physarum
-
minichromosome
-
chromatin-bound
-
endonucleolytic
-
coagulase-positive
-
coagulase-negative
-
end-labeling
-
histone-dna
- beta-globin
- drug development
- molecular biology
-
superhelical
-
supercoiled
-
exonuclease
-
dielectric
- analysis
-
i-hypersensitive
-
ladder
-
base-pairs
- biotechnology
- cscl
-
heterochromatic
-
nucleolytic
The taxonomic range for the selected organisms is: Staphylococcus aureus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
micrococcal DNase
-
-
-
-
micrococcal endonuclease
-
-
-
-
Micrococcal nuclease
MN
-
-
-
-
Nuc
NUC1
nuclease 8V
-
-
-
-
nuclease T
-
-
-
-
nuclease T'
-
-
-
-
nuclease, micrococcal
-
-
-
-
nuclease, staphylococcal
-
-
-
-
ribonucleate (deoxyribo-nucleate) 3'-nucleotidohydrolase
-
-
-
-
ribonucleate (deoxyribonucleate) 3'-nucleotidohydrolase
-
-
-
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S. aureus nuclease
-
-
-
-
snake venom phosphodiesterase
-
-
-
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SNase
spleen endonuclease
-
-
-
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spleen phosphodiesterase
-
-
-
-
staph nuclease
-
-
-
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staphylococcal nuclease
staphylococcus aureus nuclease
staphylococcus aureus nuclease B
-
-
-
-
thermonuclease
TNase
-
-
-
-
Micrococcal nuclease
-
-
-
-
SNase
-
-
-
-
SNase
-
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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
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9013-53-0
-
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
ss-DNA + H2O
?
single strand salmon sperm DNA, obtained by boiling for 30 min and rapid cooling on ice
-
-
?
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
-
-
?
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
?
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
-
-
?
additional information
?
-
-
inhibition when a 5'-phosphomonoester end group is present in an oligonucleotide
-
-
?
additional information
?
-
-
best substrates oligonucleotides with a 3'-phosphomonoester end group
-
-
?
additional information
?
-
-
substrate masking: binding of RNA by EGTA-inactivated enzyme results in artifactual inhibition of RNA processing
-
-
?
additional information
?
-
-
enzyme does not cleave the 2',3'-cyclic phosphate derivates of the ribonucleosides
-
-
?
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
-
-
?
additional information
?
-
-
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
-
-
?
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
?
-
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
?
-
-
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
?
-
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
-
-
?
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
?
-
-
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
-
-
?
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
?
-
-
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
-
-
?
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
-
-
?
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
?
-
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
additional information
Ca2+
activates to 120% of initial activity at 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 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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosine 3',5'-diphosphate
-
able to induce folding of mutant proteins into the native state
Co2+
isozyme Nuc1 shows 79% activity at 5 mM concentration
Mn2+
isozyme Nuc1 activity drops sharply at 5 mM concentration
Mn2+
isozyme Nuc2 activity decreases with an increase in Mn2+ concentration
Zn2+
isozyme Nuc1 activity drops sharply at 5 mM concentration
Zn2+
isozyme Nuc2 activity decreases with an increase in Zn2+ concentration
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
-
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
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
210.5% of initial isozyme Nuc1 activity at 1%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
1250 microg DNA/ml, construct phlbA-sp usp45-nuc, promotor phlbA, lactococcal signal peptide Usp45: sp usp45
-
additional information
additional information
-
430 microg DNA/ml, construct pusp45-sp usp45-nuc, promoter: pusp45, lactococcal signal peptide Usp45: sp usp45
-
additional information
additional information
-
P117G/H124L/S128A mutant enzyme thermodynamics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2000
-
purified recombinant enzyme, pH and temperature not specified in the publication
additional information
additional information
-
antiviral efficacy: in PK-15/Cap-SNase cells and normal PK-15 cells, infected with the classical swine fever virus Shimen strain, the virus titer produced by PK-15/Cap-SNase cells is 100 times lower than that of normal PK-15 cells 5 days after infection, after 6 days, a greater antiviral effect is observed in the PK15/Cap-SNase cells which produced a virus titer that is 3500times lower than the control
additional information
-
the activity of the 5 microl cell lysate containing Cap-SNase is similar to that of 0.5 pg of a standard preparation of SNase, while the linearized plasmid DNA can not be digested when removing Ca2+ by EDTA treatment, indicating that the expressed Cap-SNase retains a good Ca2+-dependent nuclease activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
8.8
9.5
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
effects of pH on thermonuclease activity of isozymes Nuc1 and Nuc2, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 80
effects of temperature on thermonuclease activity of isozymes Nuc1 and Nuc2, profile overview
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the isozyme Nuc2 is membrane-bound with the C-terminus facing the extracellular environment, indicating it is a signal-anchored Type II membrane protein
Staphylococcus aureus produces at least two extracellular nucleases
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
extracellular DNA promotes biofilm formation in Staphylococcus aureus and, conversely, extracellular nucleases limit the ability to form a biofilm
physiological function
additional information
malfunction
-
when the nuc1 gene is knocked out, the ability of Staphylococcus aureus strains to form a biofilm significantly increased
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
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
extracellular nucleases limit the ability to form a biofilm. The role of extracellular nucleases under in vitro versus in vivo conditions differ
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 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
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
-
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17000
17000
-
molecular weight is calculated by amino acid sequence, the Cap-SNase fusion protein with a molecular weight of 31000 Da is determines by SDS-PAGE and Western blot analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme contains 26.2% alpha-helices, 24.8% beta-sheets, 26.8% beta-turns, 8.7% unordered chains and 7.4% extended chains (6.1% is uncertain), PDB ID: 1STN
additional information
-
structural properties of the enzyme in oligomeric A-forms
additional information
-
four distinct conformational states of wild-type and mutant forms
additional information
-
solution structure of the hyperstable P117G/H124L/S128A mutant enzyme variant, overview
additional information
structure comparison of isozyme Nuc1 and Nuc2, overview
additional information
structure comparison of isozyme Nuc1 and Nuc2, overview
additional information
-
structure comparison of isozyme Nuc1 and Nuc2, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
three-dimensional diffuse x-ray scattering from crystals of the enzyme
crystal structure of binary Ca2+ and pdTp complexes of the D21E mutant enzyme
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P11A/P31A/P42A/P47T/P56A/P117G
proline free mutant, conformationally different from wild type protein, 1.4% of wild type activity
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
DELTA140-149
-
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
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
-
effects on the stability and conformation of the folded protein
H124LC80-C116
-
effects on the stability and conformation of the folded protein
I92A
-
site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme
INS33A34
-
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
P117G,/H124L/S128A
-
site-directed mutagenesis, a highly stable triple mutant
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
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
additional information
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 80
-
temperature range for studying the thermal unfolding transitions
51.7
-
melting point of K45C mutant with bound 5,5'-dithiobis-2-nitrobenzoic acid label
53
75
90
-
pH 7.9-8.8, 15 min, 20% loss of activity, pH 3.5 and 9.6, 15 min, 50% loss of activity
additional information
75
1 h, heat-treated isozyme Nuc1 is still able to degrade the DNA substrate
75
1 h, heat-treated isozyme Nuc2 is still able to degrade the DNA substrate
additional information
temperature- and pressure-dependent stability diagram, thermodynamic properties, and folding reaction kinetics of the small, single-domain monomeric staphylococcal nuclease in presence or absence of macromolecular crowder agent Ficoll PM 70, which behaves as a semi-rigid spheroid with a hydrodynamic radius of about 5 nm, detailed overview. Increasing the temperature from 25°C to 57°C exhibits no change of the size of the crowder particles within the experimentalerror. No significant changes in particle size are detected by raising the pressure up to 2.5 kbar. The measured translational diffusion times indicate that, depending on the size of the protein, themicroviscosity of Ficoll PM70 is only about 4-6 times larger than the microviscosity of pure water
additional information
-
heat-stable extracellular enzyme related structurally to a heat-labile cellular nuclease
additional information
-
2-O-alpha-mannosylglycerate protects against thermal denaturation. 0.5 M 2-O-alpha-mannosylglycerate increases Tm-value by 7.1°C. 0.5 M glycerol or trehalose increase the Tm-value by 0.8°C and 4.2°C, respectively
additional information
-
different concentrations of mannosylglycerate or presence of urea at 0.25M show no correlation with changes in the thermodynamic stability of the P117G/H124L/S128A mutant enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-O-alpha-mannosylglycerate protects against thermal denaturation, 0.5 M 2-O-alpha-mannosylglycerate increases Tm-value by 7.1°C. 0.5 M glycerol or trehalose increase the Tm-value by 0.8°C and 4.2°C, respectively
-
correlation between the magnitude of protein stabilization and the restriction of fast backbone motions, mannosylglycerate restricts local motions in addition to the global motions of the protein. Unfolding/folding pathway remain undisturbed in the presence of mannosylglycerate but the solute shows a specific effect on the local motions of beta-sheet residues
-
enzyme tryptophan fluorescence spectra, fluorescence measurements of protein unfolding under pressure, high-pressure fluorescence spectroscopy and single value decomposition analysis, overview
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
ongoing denaturation by exposure to oxidative stress brought on by illumination of a solution containing 0.145 mM enzyme and 0.5 mM fullerol with polychromatic white light
-
681601
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Lactococcus lactis cell culture medium by cation exchange chromatography
-
recombinant His-tagged truncated isozyme Nuc2 lacking the N-terminal membrane anchor by nickel-affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a plasmid pcDNA-Cap-SNase is constructed for expressing a fusion protein of classical swine fever virus capsid Cap and staphylococcal nuclease, a mammalian cell line PK-15 expressing stably the fusion protein Cap-SNase
-
expression of wild type and mutant proteins in Escherichia coli BL21(DE3), formation of inclusion bodies
-
gene nuc1, recombinant expression in Escherichia coli strain BL21(DE3)
-
gene nuc1, sequence comparison and phylogenetic analysis, functional recombinant expression in Escherichia coli strain BL21(DE3)
gene nuc1, sequence comparison, recombinant expression of C-terminally His6-tagged isozyme Nuc1 in Escherichia coli strain strain ER2566
gene nuc2, sequence comparison and phylogenetic analysis, functional recombinant expression in Escherichia coli strain BL21(DE3)
gene nuc2, sequence comparison, the portion of nuc2 encoding amino acids N26-K177 is amplified from AH1263 genomic DNA, recombinant expression of the truncated version as C-terminally His6-tagged isozyme Nuc2, and expression of isozyme Nuc2 as fusion proteins Nuc2-GFP and Nuc2-PhoA, respectively, in Escherichia coli strain strain ER2566, creating strain AH2591. Expression of recombinant chimeric His-tagged fusion proteins in Staphylococcus aureus nuc-deficient mutant strain AH1680
generation of Vibrio anguillarum ghost by coexpression of PhiX 174 Lysis E gene and SNA gene. Gene fragment encoding SNA amplified by PCR using Staphlococcus aureus genomic DNA. construction of plasmid pRK-lambda-P(R)-cI-SNA. Construction of dual vector expressing PhiX 174 lysis E gene and SNA: pRK-kP(R)-cI-E-SNA. Transformation of Escherichia coli SM10-lambda-pir used as donor for plasmid transfer with Vibrio anguillarum via conjugation. Induction of protein expression by temperature elevation
-
purification of DNA from the cell-associated herpesvirus Marek's disease virus. 150 U of Micrococcal nuclease added to gallid herpesvirus type 2 virus infected cells (GaHV-2 strain 648A) in 100 microl reaction volume, digestion followed by PEG precipitation yields high-molecular weight DNA of greater than 75% pure GaHV-2 DNA suitability for both direct pyrosequencing and further amplification using isothermal polymerase
-
SaeRS is required for expression of the nuc gene, expression from plasmid containing the nuc promoter coupled to sGFP (pCM20), transformed into the Staphylococcus aureus USA300 wild-type-LAC and sae, agr, and sigB mutant strains
-
staphylococcal nuclease fused at its N-terminus to signal peptide of the lactococcal Usp45 protein (SP Usp45-NucB), as reporter for expression and secretion in Lactobacillus bulgaricus, SDS PAGE and western blot of culture supernatant and cell lysate used for analysis
-
the enzyme is cloned into an expression-secretion vector lacking its own signal peptide but being fused to a lactococcal sequence encoding a signal peptide. It is then fused to a lactococcal sequence encoding a signal peptide. Functional recombinant expression of the enzyme under the control of a lactococcal promoter, that is inducible by zinc starvation, in Lactococcus lactis subsp. cremoris model strain MG1363, the enzyme is secreted to the GM17v culture medium, expression method optimization, overview
-
transient replication of HPV-18 mutant ori plasmids with gene-delivered chimeric mutant AZP-SNase, overexpression of recombinant mutant chimeric enzyme, hybrid nuclease AZP-SNase, in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
high concentration of urea and guanidinium chloride denaturation is completely reversible at pH 3.5-3.7, 55-65°C
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
-
generation of Vibrio anguillarum ghost by coexpression of PhiX 174 Lysis E gene and SNA gene, potential vaccine for fishes against vibriosis
medicine
-
capsid-targeted viral inactivation as an antiviral strategy against classical swine fever infection, the fusion protein Cap-SNase can inhibit effectively the production of classical swine fever virus, resulting in a reduction in infectious titers
molecular biology
analysis
-
purification of DNA from the cell-associated herpesvirus Mareks disease virus
analysis
-
staphylococcal nuclease fused at its N-terminus to signal peptide of the lactococcal Usp45 protein (SP Usp45-NucB), as reporter for expression and secretion in Lactobacillus bulgaricus
analysis
-
the enzyme is a useful tool for mapping chromatin structure in eukaryotes, usage of the enzyme to determine the positions of nucleosomes within a region of DNA to identify dynamic changes induced during gene regulation
analysis
-
combined MNase/exoIII digestion can be applied to in situ chromatin for unbiased genome-wide mapping of nucleosome positions that is not influenced by DNA sequences at the core/linker junctions. The same approach can be also used for the precise mapping of the extent of linker DNA protection by H1 and other protein factors associated with nucleosome linkers
analysis
-
the existence of MNase can be the standard to identify Staphylococcus aureus, and the content of MNase can be used to evaluate the pathogenicity of Staphylococcus aureus, usage of a graphene oxide-based biosensor, method development, overview
molecular biology
-
purified enzyme can be used as an exogenous reagent to clear cellular extracts and improve protein purification
molecular biology
-
the enzyme is a useful tool for mapping chromatin structure in eukaryotes, usage of the enzyme to determine the positions of nucleosomes within a region of DNA to identify dynamic changes induced during gene regulation
molecular biology
-
combined MNase/exoIII digestion can be applied to in situ chromatin for unbiased genome-wide mapping of nucleosome positions that is not influenced by DNA sequences at the core/linker junctions. The same approach can be also used for the precise mapping of the extent of linker DNA protection by H1 and other protein factors associated with nucleosome linkers
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JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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The purification and properties of micrococcal nuclease
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3014-3019
1961
Staphylococcus aureus
Sulkowski, E.; Laskowski, M.
Phosphatase-free crystalline micrococcal nuclease
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241
4386-4388
1966
Staphylococcus aureus, Staphylococcus aureus Foggi Worthington
Taniuchi, H.; Anfinsen, C.B.
The amino acid sequence of an extracellular nuclease of Staphylococcus aureus
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241
4366-4385
1966
Staphylococcus aureus, Staphylococcus aureus V8
Cotton, F.A.; Hazen, E.E.
Staphylococcal nuclease x-ray structure
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4
153-175
1971
Staphylococcus aureus
-
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
-
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
Wilchek, M.; Gorecki, M.
Purification of nucleases
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34
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1974
Staphylococcus aureus
Guisan, J.M.; Ballesteros, A.
Hydrolysis of nucleic acids by sepharose-micrococcal endonuclease
Enzyme Microb. Technol.
3
313-320
1981
Staphylococcus aureus
-
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
-
Vakil, B.V.; Ramakrishnan, N.; Pradhan, D.S.
Identification of a heat-labile cellular nuclease in Staphylococcus aureus with properties similar to the extracellular nuclease (EC 3.1.4.7)
Arch. Microbiol.
139
240-244
1984
Staphylococcus aureus
Cecchini, D.J.; Lin Guan, K.; Giese, R.W.
Staphylococcal nuclease high-performance liquid chromatographic characterization of diaminooctane-modified DNA and its biotin and fluorescein derivatives
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444
97-106
1988
Escherichia coli, Escherichia coli pFOG, Staphylococcus aureus
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Substrate masking: binding of RNA by EGTA-inactivated micrococcal nuclease results in artifactual inhibition of RNA processing reactions
Nucleic Acids Res.
18
6625-6631
1990
Staphylococcus aureus
Fink, A.L.; Calciano, L.J.; Goto, Y.; Nishimura, M.; Swedberg, S.A.
Characterization of the stable, acid-induced, molten globule-like state of staphylococcal nuclease
Protein Sci.
2
1155-1160
1993
Staphylococcus aureus
Libson, A.M.; Gittis, A.G.; Lattman, E.E.
Crystal structures of the binary Ca2+ and pdTp complexes and the ternary complex of the Asp21-->Glu mutant of staphylococcal nuclease. Implications for catalysis and ligand binding
Biochemistry
33
8007-8016
1994
Staphylococcus aureus
Xie, D.; Fox, R.; Freire, E.
Thermodynamic characterization of an equilibrium folding intermediate of staphylococcal nuclease
Protein Sci.
3
2175-2184
1994
Staphylococcus aureus
Eftink, M.R.; Ionescu, R.; Ramsay, G.D.; Wong, C.Y.; Wu, J.Q.; Maki, A.H.
Thermodynamics of the unfolding and spectroscopic properties of the V66W mutant of staphylococcal nuclease and its 1-136 fragment
Biochemistry
35
8084-8094
1996
Staphylococcus aureus
Wall, M.E.; Ealick, S.E.; Gruner, S.M.
Three-dimensional diffuse x-ray scattering from crystals of staphylococcal nuclease
Proc. Natl. Acad. Sci. USA
94
6180-6184
1997
Staphylococcus aureus (P00644)
Uversky, V.N.; Fink, A.L.
Structural properties of staphylococcal nuclease
Biochemistry
63
463-469
1998
Staphylococcus aureus
Hynes, T.R.; Hodel, A.; Fox, R.O.
Engineering alternative beta-turn types in staphylococcal nuclease
Biochemistry
33
5021-5030
1994
Staphylococcus aureus
Creighton, T.E.; Shortle, D.
Electrophoretic characterization of the denaturated states of staphylococcal nuclease
J. Mol. Biol.
242
670-682
1994
Staphylococcus aureus, Staphylococcus aureus Foggi Worthington
Hinck, A.P.; Truckses, D.M.; Markley, J.L.
Engineered disulfide bonds in staphylococcal nuclease: Effects on the stability and conformation of the folded protein
Biochemistry
35
10328-10338
1996
Staphylococcus aureus
Yuanhe, L.; Zhaojie, L.; Guozhong, J.
Overexpression, purification of poly-his-nuclease R and its potential use
Biotechnol. Tech.
11
729-732
1997
Staphylococcus aureus
-
Uversky, V.N.; Karnoup, A.S.; Segel, D.J.; Seshadri, S.; Doniach, S.; Fink, A.L.
Anion-induced folding of staphylococcal nuclease: characterization of multiple equilibrium partially folded intermediates
J. Mol. Biol.
278
879-894
1998
Staphylococcus aureus
Faria, T.Q.; Lima, J.C.; Bastos, M.; Macanita, A.L.; Santos, H.
Protein stabilization by osmolytes from hyperthermophiles: effect of mannosylglycerate on the thermal unfolding of recombinant nuclease a from Staphylococcus aureus studied by picosecond time-resolved fluorescence and calorimetry
J. Biol. Chem.
279
48680-48691
2004
Staphylococcus aureus
Shan, L.; Tong, Y.; Xie, T.; Wang, M.; Wang, J.
Restricted backbone conformational and motional flexibilities of loops containing peptidyl-proline bonds dominate the enzyme activity of staphylococcal nuclease
Biochemistry
46
11504-11513
2007
Staphylococcus aureus (P00644)
Maki, K.; Cheng, H.; Dolgikh, D.A.; Roder, H.
Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods
J. Mol. Biol.
368
244-255
2007
Staphylococcus aureus
Sienkiewicz, A.; Vileno, B.; Pierzchala, K.; Czuba, M.; Marcoux, P.; Graczyk, A.; Fajer, P.G.; Forro, L.
Oxidative stress-mediated protein conformation changes: ESR study of spin-labelled staphylococcal nuclease
J. Phys. Condens. Matter
19
285201/1-285201/13
2007
Staphylococcus aureus
-
Fitzkee, N.C.; Garcia-Moreno E.B.
Electrostatic effects in unfolded staphylococcal nuclease
Protein Sci.
17
216-227
2008
Staphylococcus aureus (P00644)
Onitsuka, M.; Kamikubo, H.; Yamazaki, Y.; Kataoka, M.
Mechanism of induced folding: Both folding before binding and binding before folding can be realized in staphylococcal nuclease mutants
Proteins
72
837-847
2008
Staphylococcus aureus
Chow, C.Y.; Wu, M.C.; Fang, H.J.; Hu, C.K.; Chen, H.M.; Tsong, T.Y.
Compact dimension of denatured states of staphylococcal nuclease
Proteins
72
901-909
2008
Staphylococcus aureus
Chouayekh, H.; Serror, P.; Boudebbouze, S.; Maguin, E.
Highly efficient production of the staphylococcal nuclease reporter in Lactobacillus bulgaricus governed by the promoter of the hlbA gene
FEMS Microbiol. Lett.
293
232-239
2009
Staphylococcus aureus
Volkening, J.D.; Spatz, S.J.
Purification of DNA from the cell-associated herpesvirus Mareks disease virus for 454 pyrosequencing using micrococcal nuclease digestion and polyethylene glycol precipitation
J. Virol. Methods
157
55-61
2009
Staphylococcus aureus
Kwon, S.R.; Kang, Y.J.; Lee, D.J.; Lee, E.H.; Nam, Y.K.; Kim, S.K.; Kim, K.H.
Generation of Vibrio anguillarum Ghost by Coexpression of PhiX 174 Lysis E gene and Staphylococcal Nuclease A Gene
Mol. Biotechnol.
42
154-159
2009
Staphylococcus aureus, Staphylococcus aureus KCCM 11335
Zhou, B.; Liu, K.; Wei, J.C.; Mao, X.; Chen, P.Y.
Inhibition of replication of classical swine fever virus in a stable cell line by the viral capsid and Staphylococcus aureus nuclease fusion protein
J. Virol. Methods
167
79-83
2010
Staphylococcus aureus
Wang, C.C.; Tsong, T.Y.; Hsu, Y.H.; Marszalek, P.E.
Inhibitor binding increases the mechanical stability of staphylococcal nuclease
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100
1094-1099
2011
Staphylococcus aureus
Li, L.; Arnosti, D.
Fine mapping of chromatin structure in Drosophila melanogaster embryos using micrococcal nuclease
Fly
4
213-215
2010
Staphylococcus aureus
Berends, E.T.; Horswill, A.R.; Haste, N.M.; Monestier, M.; Nizet, V.; von Koeckritz-Blickwede, M.
Nuclease expression by Staphylococcus aureus facilitates escape from neutrophil extracellular traps
J. Innate Immun.
2
576-586
2010
Staphylococcus aureus, Staphylococcus aureus USA 300 LAC
Tremillon, N.; Issaly, N.; Mozo, J.; Duvignau, T.; Ginisty, H.; Devic, E.; Poquet, I.
Production and purification of staphylococcal nuclease in Lactococcus lactis using a new expression-secretion system and a pH-regulated mini-reactor
Microb. Cell Fact.
9
37
2010
Staphylococcus aureus
Tang, J.; Kang, M.; Chen, H.; Shi, X.; Zhou, R.; Chen, J.; Du, Y.
The staphylococcal nuclease prevents biofilm formation in Staphylococcus aureus and other biofilm-forming bacteria
Sci. China Life Sci.
54
863-869
2011
Staphylococcus aureus, Staphylococcus aureus RN4220
Peng, Y.; Jiang, J.; Yu, R.
Label-free and sensitive detection of micrococcal nuclease activity using DNA-scaffolded silver nanoclusters as a fluorescence indicator
Anal. Methods
6
4090-4094
2014
Staphylococcus aureus
-
Wang, S.; Tate, M.W.; Gruner, S.M.
Protein crowding impedes pressure-induced unfolding of staphylococcal nuclease
Biochim. Biophys. Acta
1820
957-961
2012
Staphylococcus aureus
Talla, D.; Stites, W.E.
The fluorescence detected guanidine hydrochloride equilibrium denaturation of wild-type staphylococcal nuclease does not fit a three-state unfolding model
Biochimie
95
1386-1393
2013
Staphylococcus aureus
Spencer, D.; Bertrand, G.M.; Stites, W.E.
The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model
Biophys. Chem.
180-181
86-94
2013
Staphylococcus aureus
He, Y.; Xiong, L.H.; Xing, X.J.; Tang, H.W.; Pang, D.W.
An ultra-high sensitive platform for fluorescence detection of micrococcal nuclease based on graphene oxide
Biosens. Bioelectron.
42
467-473
2013
Staphylococcus aureus, Staphylococcus aureus CCTCC AB91093
Beenken, K.E.; Spencer, H.; Griffin, L.M.; Smeltzer, M.S.
Impact of extracellular nuclease production on the biofilm phenotype of Staphylococcus aureus under in vitro and in vivo conditions
Infect. Immun.
80
1634-1638
2012
Staphylococcus aureus (A0A0H3JPX6), Staphylococcus aureus (Q7A6P2), Staphylococcus aureus N315 (Q7A6P2)
Olson, M.E.; Nygaard, T.K.; Ackermann, L.; Watkins, R.L.; Zurek, O.W.; Pallister, K.B.; Griffith, S.; Kiedrowski, M.R.; Flack, C.E.; Kavanaugh, J.S.; Kreiswirth, B.N.; Horswill, A.R.; Voyich, J.M.
Staphylococcus aureus nuclease is an SaeRS-dependent virulence factor
Infect. Immun.
81
1316-1324
2013
Staphylococcus aureus
Allan, J.; Fraser, R.M.; Owen-Hughes, T.; Keszenman-Pereyra, D.
Micrococcal nuclease does not substantially bias nucleosome mapping
J. Mol. Biol.
417
152-164
2012
Staphylococcus aureus (P00644)
Nikitina, T.; Wang, D.; Gomberg, M.; Grigoryev, S.A.; Zhurkin, V.B.
Combined micrococcal nuclease and exonuclease III digestion reveals precise positions of the nucleosome core/linker junctions: implications for high-resolution nucleosome mapping
J. Mol. Biol.
425
1946-1960
2013
Staphylococcus aureus
Hu, Y.; Meng, J.; Shi, C.; Hervin, K.; Fratamico, P.M.; Shi, X.
Characterization and comparative analysis of a second thermonuclease from Staphylococcus aureus
Microbiol. Res.
168
174-182
2013
Staphylococcus aureus (A0A0H3JPX6), Staphylococcus aureus (Q7A6P2), Staphylococcus aureus, Staphylococcus aureus N315 (Q7A6P2)
Erlkamp, M.; Grobelny, S.; Winter, R.
Crowding effects on the temperature and pressure dependent structure, stability and folding kinetics of Staphylococcal nuclease
Phys. Chem. Chem. Phys.
16
5965-5976
2014
Staphylococcus aureus (P00644)
Mino, T.; Mori, T.; Aoyama, Y.; Sera, T.
Gene- and protein-delivered zinc finger-staphylococcal nuclease hybrid for inhibition of DNA replication of human papillomavirus
PLoS ONE
8
e56633
2013
Staphylococcus aureus
Kiedrowski, M.R.; Crosby, H.A.; Hernandez, F.J.; Malone, C.L.; McNamara, J.O.; Horswill, A.R.
Staphylococcus aureus Nuc2 is a functional, surface-attached extracellular nuclease
PLoS ONE
9
e95574
2014
Staphylococcus aureus (A0A0H3JPX6), Staphylococcus aureus (Q7A6P2), Staphylococcus aureus N315 (A0A0H3JPX6), Staphylococcus aureus N315 (Q7A6P2)
Pais, T.M.; Lamosa, P.; Matzapetakis, M.; Turner, D.L.; Santos, H.
Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow beta-sheet motions
Protein Sci.
21
1126-1137
2012
Staphylococcus aureus
Roche, J.; Caro, J.A.; Dellarole, M.; Guca, E.; Royer, C.A.; Garcia-Moreno, B.E.; Garcia, A.E.; Roumestand, C.
Structural, energetic, and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity-creating mutations
Proteins
81
1069-1080
2013
Staphylococcus aureus
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