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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
- deoxyribonuclease
- nucleoprotein
- enterotoxin
-
footprint
-
internucleosomal
- ribonucleoprotein
-
oligonucleosomes
-
octamer
-
nonhistone
- dnaase
-
coagulase
-
nucleolytic
- medicine
- globin
-
hyperacetylated
-
dielectric
-
end-labeling
- polycephalum
-
supercoiled
-
histone-dna
-
heterochromatic
-
protein-dna
-
chromatin-associated
-
i-hypersensitive
- analysis
-
minichromosome
-
superhelical
-
snrnp
-
exonuclease
-
centromeres
-
native-like
-
decondensation
-
chromatin-bound
-
coagulase-positive
-
base-pairs
- physarum
- molecular biology
- biotechnology
-
staphylococci
-
endonucleolytic
-
nuclease-resistant
- beta-globin
-
32p-postlabeling
- drug development
-
ladder
-
telomeres
- cscl
-
non-transcribed
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products
Synonyms
AtTSN1, AtTSN2, cTSN, EC 3.1.4.7, Epstein-Barr virusencoded transcription factor 2 co-activator p100, HsTSN, micrococcal DNase, micrococcal endonuclease, Micrococcal nuclease, MN, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.1.4.7
-
-
formerly
-
micrococcal DNase
-
-
-
-
micrococcal endonuclease
-
-
-
-
Micrococcal nuclease
MN
-
-
-
-
MNase
Nuc
NUC1
Nuc2
nuclease 8V
-
-
-
-
nuclease T
-
-
-
-
nuclease T'
-
-
-
-
nuclease, micrococcal
-
-
-
-
nuclease, staphylococcal
-
-
-
-
NucM
ribonucleate (deoxyribo-nucleate) 3'-nucleotidohydrolase
-
-
-
-
ribonucleate (deoxyribonucleate) 3'-nucleotidohydrolase
-
-
-
-
S. aureus nuclease
-
-
-
-
SNA
snake venom phosphodiesterase
-
-
-
-
SNase
SNAseR
-
analogue of SNAse A EC 3.1.4.7, in which hexapeptide is appended to the alanine of SNAse A
SND1
spleen endonuclease
-
-
-
-
spleen phosphodiesterase
-
-
-
-
staph nuclease
-
-
-
-
staphylococcal nuclease
Staphylococcal nuclease A
staphylococcus aureus nuclease
staphylococcus aureus nuclease B
-
-
-
-
thermonuclease
TNase
-
-
-
-
TSN
tudor staphylococcal nuclease
Micrococcal nuclease
-
-
-
-
SNase
-
-
-
-
SNase
-
-
SNase
-
-
staphylococcal nuclease
-
-
-
-
staphylococcal nuclease
-
-
staphylococcal nuclease
-
-
staphylococcus aureus nuclease
-
-
-
-
staphylococcus aureus nuclease
-
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
hydrolysis of phosphoric ester
-
-
-
-
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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
-
-
?
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
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
?
-
substrates are double-stranded RNA targeting PAZ domain of PmAgo1, PmRab7, and gfp. The enzyme shows calcium-dependent RNase activity, overview
-
-
-
additional information
?
-
-
substrates are double-stranded RNA targeting PAZ domain of PmAgo1, PmRab7, and gfp. The enzyme shows calcium-dependent RNase activity, overview
-
-
-
additional information
?
-
-
essential enzyme in the life cycle of Plasmodium falciparum
-
-
-
additional information
?
-
-
GFP-dsDNA and GFP-dsRNA are not used as substrates
-
-
-
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
?
-
Q7A5U0
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
?
-
Q7A5U0
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
?
-
-
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
?
-
Q7A5U0
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
?
-
-
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
?
-
Q7A5U0
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
?
-
-
substrate is single-strand salmon sperm DNA
-
-
-
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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
?
-
G1ARD5
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+
-
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
Q7A5U0
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
Q7A5U0
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%
-
deoxythymidine 3',5'-diphosphate
-
in the presence of pdTp, unfolding forces increase drastically
Mn2+
Q7A5U0, Q7A6P2
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+
Q7A5U0, Q7A6P2
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
Q7A5U0
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
NaCl
-
maximum activity of SNR140 and SNR141 SNAse R N-terminal fragments which extends from residues 6 to 140 and 6 to 141 respectively, 0.3 M, studies performed to explore the mechanism of nascent peptide folding
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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; 430 microg DNA/ml, construct pusp45-sp usp45-nuc, promoter: pusp45, lactococcal signal peptide Usp45: sp usp45
-
additional information
additional information
-
Michaelis-Menten kinetics for wild-type SNase and its mutants, overview
-
additional information
additional information
-
P117G/H124L/S128A mutant enzyme thermodynamics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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; 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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
8.8
10
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 8
-
the overall secondary and tertiary structure of SNase remains unchanged between pH 2.5 and 8.0
3 - 10
Q7A5U0, Q7A6P2
effects of pH on thermonuclease activity of isozymes Nuc1 and Nuc2, profile overview; effects of pH on thermonuclease activity of isozymes Nuc1 and Nuc2, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 80
Q7A5U0, Q7A6P2
effects of temperature on thermonuclease activity of isozymes Nuc1 and Nuc2, profile overview; effects of temperature on thermonuclease activity of isozymes Nuc1 and Nuc2, profile overview
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
complementation of the Lactococcus lactis secretion machinery with Bacillus subtilis SecDF improves secretion of staphylococcal nuclease
-
-
brenda
strains 3D7 and W2mef, enzyme expressed in all three blood stages: ring, trophozoite and schizont stage
-
-
brenda
-
135024, 135025, 135026, 135027, 135028, 135030, 135031, 135032, 135035, 135037, 135038, 135043, 135044, 135046, 135047, 135048, 665585, 681601, 682778, 697993, 699892, 705421, 717383, 717620, 718081, 728958, 729277, 729335, 729399, 729448, 730213, 730723, 730894, 730910, 730986
-
-
brenda
; mutants L25A L36A 61G62 I72A 90P91 Y91A I92A Y93A 94A95 L103G 103A104 G107V L108A L125A L125G
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-
brenda
gene nuc1; different USA300 strains, SF8300 and LAC, RN4220, MW2, TCH1516, COL and UAMS-1, gene nuc1
UniProt
brenda
gene nuc2; different USA300 strains, SF8300 and LAC, RN4220, MW2, TCH1516, COL and UAMS-1, gene nuc2
Q7A5U0
UniProt
brenda
native state protein and engineered proteins showing a disordered state under physiological conditions
-
-
brenda
gene nuc1; different USA300 strains, SF8300 and LAC, RN4220, MW2, TCH1516, COL and UAMS-1, gene nuc1
UniProt
brenda
gene nuc2; different USA300 strains, SF8300 and LAC, RN4220, MW2, TCH1516, COL and UAMS-1, gene nuc2
Q7A5U0
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
expression of the enzyme and of angiotensin II type 1 receptor are positively correlated
brenda
-
Staphylococcal nuclease domain containing-1 is overexpressed in human hepatocellular carcinoma patients
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
human Tudor staphylococcal nuclease interacts with the Ras-GAP SH3 domain-binding protein and is recruited into stress granules, the main type of discrete RNA-containing cytoplasmic foci structure that is formed under stress conditions
-
brenda
in the interphase and mitosis; in the interphase and mitosis
brenda
-
during trophozoite and schizont stages parts of enzyme localized in the cytoplasm
brenda
Q7A5U0, Q7A6P2
Staphylococcus aureus produces at least two extracellular nucleases; Staphylococcus aureus produces at least two extracellular nucleases
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brenda
-
; Staphylococcus aureus produces at least two extracellular nucleases
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-
brenda
Q7A5U0, Q7A6P2
the isozyme Nuc2 is membrane-bound with the C-terminus facing the extracellular environment, indicating it is a signal-anchored Type II membrane protein
brenda
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the isozyme Nuc2 is membrane-bound with the C-terminus facing the extracellular environment, indicating it is a signal-anchored Type II membrane protein
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brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
A0A076JRM7, A0A076JSR1, A0A076JWH6
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; 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; 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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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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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
-
malfunction
-
when the nuc1 gene is knocked out, the ability of Staphylococcus aureus strains to form a biofilm significantly increased
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
Q7A5U0, Q7A6P2
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; 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
-
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. The susceptibility to daptomycin is reduced in the mutants
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malfunction
-
when the nuc1 gene is knocked out, the ability of Staphylococcus aureus strains to form a biofilm significantly increased
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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
Q7A5U0, Q7A6P2
extracellular DNA promotes biofilm formation in Staphylococcus aureus and, conversely, extracellular nucleases limit the ability to form a biofilm; extracellular DNA promotes biofilm formation in Staphylococcus aureus and, conversely, extracellular nucleases limit the ability to form a biofilm
metabolism
-
extracellular DNA promotes biofilm formation in Staphylococcus aureus and, conversely, extracellular nucleases limit the ability to form a biofilm
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physiological function
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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
-
Staphylococcal nuclease degrades both DNA and RNA
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
-
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
-
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
-
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
-
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
involvement of PmAgo1 and the enzyme in shrimp RNAi pathway, RNAi-based mechanism in shrimp, overview
physiological function
Q7A5U0, Q7A6P2
extracellular nucleases limit the ability to form a biofilm. The role of extracellular nucleases under in vitro versus in vivo conditions differ; extracellular nucleases limit the ability to form a biofilm. The role of extracellular nucleases under in vitro versus in vivo conditions differ
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
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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
Q7A5U0, Q7A6P2
major role for isozyme Nuc1 in terms of thermonuclease activity
physiological function
Q7A5U0, Q7A6P2
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
-
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
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extracellular nucleases limit the ability to form a biofilm. The role of extracellular nucleases under in vitro versus in vivo conditions differ; isozyme Nuc2 is detrimental to Staphylococcus aureus biofilms, purified isozyme Nuc2 prevents biofilm formation in vitro and modestly decreases biomass in dispersal experiments; major role for isozyme Nuc1 in terms of thermonuclease activity
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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
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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
-
additional information
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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
-
residue W140 is critical to SNase structure and function
additional information
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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
-
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 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
-
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
-
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
Q7A5U0
sequence and structure comparisons of isozymes Nuc1 and Nuc2, overview; sequence and structure comparisons of isozymes Nuc1 and Nuc2, overview
additional information
sequence and structure comparisons of isozymes Nuc1 and Nuc2, overview; sequence and structure comparisons of isozymes Nuc1 and Nuc2, overview
additional information
-
mannosylglycerate preferentially affects specific structural elements of the P117G/H124L/S128A mutant enzyme, structure analysis, overview
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; sequence and structure comparisons of isozymes Nuc1 and Nuc2, overview
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Show AA Sequence and Transmembrane Helices (1129 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16800
17000
95000
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x * 95000, SDS-PAGE of the recombinant fusion protein with Maltose Binding Protein
120000
x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE
126000
x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE
17000
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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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer or dimer
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small globular protein (149 amino acid residues), native protein: no disulfide bond, double mutant (A1C/Q149C): can form disulfide bond
additional information
?
x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE
?
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x * 110000, SDS-PAGE, native protein; x * 95000, SDS-PAGE of the recombinant fusion protein with Maltose Binding Protein
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
Q7A5U0
structure comparison of isozyme Nuc1 and Nuc2, overview; structure comparison of isozyme Nuc1 and Nuc2, overview
additional information
structure comparison of isozyme Nuc1 and Nuc2, overview; structure comparison of isozyme Nuc1 and Nuc2, overview
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
-
solution structure of the hyperstable P117G/H124L/S128A mutant enzyme variant, overview
additional information
-
four distinct conformational states of wild-type and mutant forms
-
additional information
-
structure comparison of isozyme Nuc1 and Nuc2, overview
-
additional information
-
secondary structure of SNase and its mutants, W140A and Y93W/W140A have less alpha-helical content than the wild-type, overview
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystal structure of binary Ca2+ and pdTp complexes of the D21E mutant enzyme
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three-dimensional diffuse x-ray scattering from crystals of the enzyme
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crystals of the hyperstable mutant enzyme delta+PHS are grown using hanging drop vapor-diffusion methods at 4°C from a solution containing 17% 2-methyl-2,4-pentanediol, 2 M CaCl2, 3 M thymine-3',5'-diphosphate, and 25 mM potassium phosphate buffer, pH 8.0
-
crystals of the I92E and I92K variant proteins are obtained at 4°C using the hanging-drop vapor-diffusion method
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E75A mutant: 4°C, hanging-drop, precipitating solution 37% (v/v) 2-methyl-2,4-pentanediol and 25 mM potassium phosphate buffer at pH 6.0, protein concentration 9.9 mg/ml before mixing with equal volume of precipitating solution. E75Q: 4°C, hanging-drop, precipitating solution 38% (v/v) 2-methyl-2,4-pentanediol and 25 mM potassium phosphate buffer at pH 6.0, starting from 14.2 mg/ml protein. Side chain of His121 is unaffected by elimination of Glu75, histidine moves closer to Glu101 in the structure with E75A. Both crystal structures suggest that the network of polar or ionizable groups connected through hydrogen bonding or charge-charge interactions is a rigid unit, incapable of reorganizing even when strongly stabilizing interactions between Glu75, His124, and Tyr93 are disrupted
-
LMYKGQPM, short peptide model from staphylococcal nuclease to model the conformational equilibrium between a hairpin conformation and its unfolded state (molecular dynamics simulation), in water, cubic model system, total simulation time 600 ns, starting from a polyproline II conformation, GROMOS96 force field under NVT conditions, 27°C: native and non-native hairpins are very close in free energies, interconversion can happen only through the unfolded conformation. Both folding and unfolding events display single exponential kinetics
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the V66K/P117G/H124L/S128A variant of nuclease is crystallized by the hanging drop vapor diffusion method at 4°C, 2 data sets are collected at -173.15°C, at pH 7 and 4.7, and the third is collected at 25.15°C and pH 5
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
G79S/H124LC80-C116
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effects on the stability and conformation of the folded protein
H124LC77-C118
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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
P117G,/H124L/S128A
-
site-directed mutagenesis, a highly stable triple mutant
P11A/P31A/P42A/P47T/P56A/P117G
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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
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
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
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
D77G
D77N
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
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
E73G/D77G
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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
E75Q
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
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
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)
K133A
-
intact tertiary conformation, melting point is 4.6°C lower than that of the wild-type enzyme
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
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
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
W140A
W140F
W140H
W140L
W140Y
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
additional information
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
-
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
-
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
-
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
-
native-like structure and native-like activity under physiological conditions
W140H
-
native-like structure and native-like activity under physiological conditions
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
-
suppression in QGY-7703 cells by si RNA, SND1-17-AT1Rsi
additional information
-
knockdown of SND1 in QGY-7703 cells inhibits establishment of xenografts in nude mice
additional information
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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
Q7A5U0
generation of a nuc1/nuc2 double deletion mutant; generation of a nuc1/nuc2 double deletion mutant
additional information
generation of a nuc1/nuc2 double deletion mutant; generation of a nuc1/nuc2 double deletion mutant
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
Q7A5U0
construction of nuc1 and nuc1/nuc2 deletion mutant strains; 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; 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
-
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
-
construction of nuc1 and nuc1/nuc2 deletion mutant strains; 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; 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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 9
-
measurement of stability by two methods: first fluorescence-monitored denaturation with urea, hydrochloric acid and heat. Second by numerical integration of acid titration curves measured potentiometrically under native and unfolding conditions
657910
4.15
-
pH-value, at which the acid-denaturation is half completed in wild-type enzyme
664352
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15 - 80
-
temperature range for studying the thermal unfolding transitions
39
-
Tm-value of mutant enzyme W140F is 39.1°C, Tm-value of mutant enzyme W140Y is 38.6°C
48
51
51.7
-
melting point of K45C mutant with bound 5,5'-dithiobis-2-nitrobenzoic acid label
53
75
Q7A5U0, Q7A6P2
1 h, heat-treated isozyme Nuc1 is still able to degrade the DNA substrate; 1 h, heat-treated isozyme Nuc2 is still able to degrade the DNA substrate
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
53
-
melting point of the Trp102 insertion mutant enzyme; melting point of the Trp61 insertion mutant enzyme
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
-
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
-
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
additional information
-
examination of denaturation (monitored by intrinsic fluorescence of Trp140) due to heat (pH 7): D21N/T33V/T41I/S59A/P117G/A128A mutant(Tm = 72°C), K9A mutant (Tm = 71°C), E73A mutant (Tm = 67°C), E75A mutant (Tm = 70°C), E75Q mutant (Tm = 70°C), D77A mutant (Tm = 67°C), Y91A mutant (Tm = 58°C), Y93A mutant (Tm = 52°C), E101A mutant (Tm = 71°C), K127A mutant (Tm = 75°C), A128S mutant (Tm = 71°C)
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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
-
denaturation midpoint for urea is 1.5 M for mutant G20A, 1.1 M urea for mutant G20V, 0.82 Murea or mutant G20I and 2.0 M for wild-type enzyme
-
denaturation of staphylococcal nuclease is induced by guanidinium hydrochloride, wild type and unlabeled mutant proteins are denatured in 20 mM Tris-HCl containing 0.1 M NaCl, pH 7.6 and 10 mM CaCl2, containing various concentrations of guanidinium hydrochloride at 25°C for 20 h to reach equilibrium
-
enzyme tryptophan fluorescence spectra, fluorescence measurements of protein unfolding under pressure, high-pressure fluorescence spectroscopy and single value decomposition analysis, overview
-