アスペルギルスヌクレアーゼS1
WordNet
- the 19th letter of the Roman alphabet (同)s
- general term for enzymes that catalyze the hydrolysis of nucleic acid by cleaving chains of nucleotides into smaller units
- genus of common molds causing food spoilage and some pathogenic to plants and animals (同)genus Aspergillus
PrepTutorEJDIC
- sulfurの化学記号 / {略}South[ern]
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/10/12 20:51:38」(JST)
[Wiki en表示]
Aspergillus nuclease S1 |
Identifiers |
EC number |
3.1.30.1 |
CAS number |
37288-25-8 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
|
Aspergillus nuclease S1 is an endonuclease enzyme derived from Aspergillus oryzae that splits single-stranded DNA (ssDNA) and RNA into oligo- or mononucleotides. This enzyme catalyses the following chemical reaction
- Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products
Although its primary substrate is single-stranded, it can also occasionally introduce single-stranded breaks in double-stranded DNA or RNA, or DNA-RNA hybrids. The enzyme hydrolyses single stranded region in duplex DNA such as loops or gaps.
Contents
- 1 Nomenclature
- 2 Properties
- 3 Uses
- 4 References
Nomenclature[edit]
Alternative names include EC 3.1.30.1, endonuclease S1 (Aspergillus), single-stranded-nucleate endonuclease, deoxyribonuclease S1, deoxyribonuclease S1, nuclease S1, Neurospora crassa single-strand specific endonuclease, S1 nuclease, single-strand endodeoxyribonuclease, single-stranded DNA specific endonuclease, single-strand-specific endodeoxyribonuclease, single strand-specific DNase and Aspergillus oryzae S1 nuclease.
Properties[edit]
Aspergillus nuclease S1 is a monomeric protein of a molecular weight of 38 kilodalton. It requires Zn2+ as a cofactor and is relatively stable against denaturing agents like urea, SDS, or formaldehyde. The optimum pH for its activity lies between 4-4.5. Aspergillus nuclease S1 is known to be inhibited somewhat by 50 μM ATP and nearly completely by 1 mM ATP.[1][2] 50% inhibition has been shown at 85 μM dAMP and 1 μM dATP but uninhibited by cAMP.[3]
Uses[edit]
Aspergillus nuclease S1 is used in the laboratory as a reagent in nuclease protection assays. In molecular biology, it is used in removing single stranded tails from DNA molecules to create blunt ended molecules and opening hairpin loops generated during synthesis of double stranded cDNA.
References[edit]
- ^ Yang, Xinjian; Fang Pu, Jinsong Ren, Xiaogang Qu (2011). "DNA-templated ensemble for label-free and real-time fluoresence turn-on detection of enzymatic/oxidative cleavage of single-stranded DNA". Chemical Communications 47: 8133–8135.
- ^ Wrede, Paul; Alexander Rich (1979). "Stability of the unique anticodon loop conformation of E.Col tRNAMetf". Nucleic Acids Research 7 (6).
- ^ Wiegand, RC; GN Godson, CM Radding (1975). "Specificity of the S1 nuclease from Aspergilus oryzae". The Journal of Biological Chemistry 250 (22).
Hydrolase: esterases (EC 3.1)
|
|
3.1.1: Carboxylic ester hydrolases |
- Cholinesterase
- Acetylcholinesterase
- Butyrylcholinesterase
- Pectinesterase
- 6-phosphogluconolactonase
- PAF acetylhydrolase
- Lipase
- Bile salt-dependent
- Gastric/Lingual
- Pancreatic
- Lysosomal
- Hormone-sensitive
- Endothelial
- Hepatic
- Lipoprotein
- Monoacylglycerol
- Diacylglycerol
|
|
3.1.2: Thioesterase |
- Palmitoyl protein thioesterase
- Ubiquitin carboxy-terminal hydrolase L1
|
|
3.1.3: Phosphatase |
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Phosphoprotein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Phosphoprotein phosphatase: Protein tyrosine phosphatase
- Protein serine/threonine phosphatase
- Dual-specificity phosphatase
|
|
3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- PDE1
- PDE2
- PDE3
- PDE4A/PDE4B
- PDE5
- Lecithinase (Clostridium perfringens alpha toxin)
- Cyclic nucleotide phosphodiesterase
|
|
3.1.6: Sulfatase |
- arylsulfatase
- Arylsulfatase A
- Arylsulfatase B
- Arylsulfatase E
- Steroid sulfatase
- Galactosamine-6 sulfatase
- Iduronate-2-sulfatase
- N-acetylglucosamine-6-sulfatase
|
|
Nuclease (includes
deoxyribonuclease and
ribonuclease) |
3.1.11-16: Exonuclease |
Exodeoxyribonuclease |
|
|
Exoribonuclease |
|
|
|
3.1.21-31: Endonuclease |
Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
|
|
Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
|
|
either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
|
|
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
English Journal
- Dexamethasone partially rescues ataxia telangiectasia-mutated (ATM) deficiency in ataxia telangiectasia by promoting a shortened protein variant retaining kinase activity.
- Menotta M, Biagiotti S, Bianchi M, Chessa L, Magnani M.Author information Department of Biomolecular Sciences, University of Urbino Carlo Bo, 61029 Urbino, Italy. michele.menotta@uniurb.itAbstractAtaxia telangiectasia (AT) is a rare genetic disease, still incurable, resulting from biallelic mutations in the ataxia telangiectasia-mutated (ATM) gene. Recently, short term treatment with glucocorticoid analogues improved neurological symptoms characteristic of this syndrome. Nevertheless, the molecular mechanism involved in glucocorticoid action in AT patients is not yet known. Here we describe, for the first time in mammalian cells, a short direct repeat-mediated noncanonical splicing event induced by dexamethasone, which leads to the skipping of mutations upstream of nucleotide residue 8450 of ATM coding sequence. The resulting transcript provides an alternative ORF translated in a new ATM variant with the complete kinase domain. This miniATM variant was also highlighted in lymphoblastoid cell lines from AT patients and was shown to be likely active. In conclusion, dexamethasone treatment may partly restore ATM activity in ataxia telangiectasia cells by a new molecular mechanism that overcomes most of the mutations so far described within this gene.
- The Journal of biological chemistry.J Biol Chem.2012 Nov 30;287(49):41352-63. doi: 10.1074/jbc.M112.344473. Epub 2012 Oct 10.
- Ataxia telangiectasia (AT) is a rare genetic disease, still incurable, resulting from biallelic mutations in the ataxia telangiectasia-mutated (ATM) gene. Recently, short term treatment with glucocorticoid analogues improved neurological symptoms characteristic of this syndrome. Nevertheless, the mo
- PMID 23055520
- A comprehensive analysis of precursor microRNA cleavage by human Dicer.
- Feng Y, Zhang X, Graves P, Zeng Y.Author information Department of Pharmacology, University of Minnesota, Minneapolis, Minnesota 55455, USA.AbstractDicer cleaves double-stranded RNAs (dsRNAs) or precursor microRNAs (pre-miRNAs) to yield ≈ 22-nt RNA duplexes. The pre-miRNA structure requirement for human Dicer activity is incompletely understood. By large-scale in vitro dicing assays and mutagenesis studies, we showed that human Dicer cleaves most, although not all, of the 161 tested human pre-miRNAs efficiently. The stable association of RNAs with Dicer, as examined by gel shift assays, appears important but is not sufficient for cleavage. Human Dicer tolerates remarkable structural variation in its pre-miRNA substrates, although the dsRNA feature in the stem region and the 2-nt 3'-overhang structure in a pre-miRNA contribute to its binding and cleavage by Dicer, and a large terminal loop further enhances pre-miRNA cleavage. Dicer binding protects the terminal loop from digestion by S1 nuclease, suggesting that Dicer interacts directly with the terminal loop region.
- RNA (New York, N.Y.).RNA.2012 Nov;18(11):2083-92. doi: 10.1261/rna.033688.112. Epub 2012 Sep 14.
- Dicer cleaves double-stranded RNAs (dsRNAs) or precursor microRNAs (pre-miRNAs) to yield ≈ 22-nt RNA duplexes. The pre-miRNA structure requirement for human Dicer activity is incompletely understood. By large-scale in vitro dicing assays and mutagenesis studies, we showed that human Dicer cleaves
- PMID 22984192
- Protein switches identified from diverse insertion libraries created using S1 nuclease digestion of supercoiled-form plasmid DNA.
- Tullman J, Guntas G, Dumont M, Ostermeier M.Author information Department of Chemical and Biomolecular Engineering, Johns Hopkins University, 3400N. Charles St., Baltimore, Maryland 21218, USA.AbstractWe demonstrate that S1 nuclease converts supercoiled plasmid DNA to unit-length, linear dsDNA through the creation of a single, double-stranded break in a plasmid molecule. These double-stranded breaks occur not only in the origin of replication near inverted repeats but also at a wide variety of locations throughout the plasmid. S1 nuclease exhibits this activity under conditions typically employed for the nuclease's single-stranded nuclease activity. Thus, S1 nuclease digestion of plasmid DNA, unlike analogous digestion with DNaseI, effectively halts after the first double-stranded break. This property makes easier the construction of large domain insertion libraries in which the goal is to insert linear DNA at a variety of locations throughout a plasmid. We used this property to create a library in which a circularly permuted TEM1 β-lactamase gene was inserted throughout a plasmid containing the gene encoding Escherichia coli ribose binding protein. Gene fusions that encode allosteric switch proteins in which ribose modulates β-lactamase catalytic activity were isolated from this library using a combination of a genetic selection and a screen.
- Biotechnology and bioengineering.Biotechnol Bioeng.2011 Nov;108(11):2535-43. doi: 10.1002/bit.23224. Epub 2011 Jun 15.
- We demonstrate that S1 nuclease converts supercoiled plasmid DNA to unit-length, linear dsDNA through the creation of a single, double-stranded break in a plasmid molecule. These double-stranded breaks occur not only in the origin of replication near inverted repeats but also at a wide variety of lo
- PMID 21618478
Japanese Journal
- Aspergillus oryzaeのS1ヌクレア-ゼ遺伝子(nucS)のクロ-ニングと構造解析ならびに高発現
- Cloning, characterization and overproduction of nuclease S1 gene (nucS) from Aspergillus oryzae
Related Links
- Source: Aspergillus oryzae I.U.B.: 3.1.30.1 Nuclease S1 isolated from certain Neurospora and Aspergillus species specifically hydrolyzes both terminal and internal phosphodiester bonds of single-stranded DNA and RNA. Nuclease ...
- Nuclease S1 from Aspergillus oryzae Product Number N 5661 Storage Temperature –20 C EC 3.1.30.1 CAS# 37288-25-8 Product Description Nuclease S1 isolated from Aspergillus oryzae exhibits endo- and exolytic hydrolytic ...
Related Pictures
★リンクテーブル★
[★]
- 英
- S1 nuclease
- 関
- アスペルギルスヌクレアーゼS1 Aspergillus nuclease S1
[★]
- 英
- Aspergillus nuclease S1
- 関
- S1ヌクレアーゼ
[★]
ヌクレアーゼ、核酸分解酵素
[★]
[★]
アスペルギルス属