小球菌ヌクレアーゼ
WordNet
- general term for enzymes that catalyze the hydrolysis of nucleic acid by cleaving chains of nucleotides into smaller units
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/03/29 20:36:36」(JST)
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| Micrococcal nuclease |
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Ribbon schematic of micrococcal nuclease 3D structure, with Ca2+ and TdtP inhibitor
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| Identifiers |
| EC number |
3.1.31.1 |
| CAS number |
9013-53-0 |
| 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 |
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Micrococcal Nuclease (EC 3.1.31.1, S7 Nuclease, MNase, spleen endonuclease, thermonuclease, nuclease T, micrococcal endonuclease, nuclease T', staphylococcal nuclease, spleen phosphodiesterase, Staphylococcus aureus nuclease, Staphylococcus aureus nuclease B, ribonucleate (deoxynucleate) 3'-nucleotidohydrolase) is an endo-exonuclease that preferentially digests single-stranded nucleic acids. The rate of cleavage is 30 times greater at the 5' side of A or T than at G or C and results in the production of mononucleotides and oligonucleotides with terminal 3'-phosphates. The enzyme is also active against double-stranded DNA and RNA and all sequences will be ultimately cleaved.
Contents
- 1 Characteristics
- 2 Sources
- 3 Structure
- 4 Applications
- 5 References
- 6 External links
Characteristics
The enzyme has a molecular weight of 16.9kDa.
The pH optimum is reported as 9.2. The enzyme activity is strictly dependent on Ca2+ and the pH optimum varies according to Ca2+ concentration.[1] The enzyme is therefore easily inactivated by EGTA.
Sources
This enzyme is the extracellular nuclease of Staphylococcus aureus. Two strains, V8 and Foggi, yield almost identical enzymes.[2] A common source is E.coli cells carrying a cloned nuc gene encoding Staphylococcus aureus extracellular nuclease (micrococcal nuclease).
Structure
The 3-dimensional structure of micrococcal nuclease (then called Staphyloccal nuclease) was solved very early in the history of protein crystallography, in 1969,[3] deposited as now-obsolete Protein Data Bank file 1SNS. Higher-resolution, more recent crystal structures are available for the apo form as Protein Data Bank file 1SNO: [1] and for the thymidine-diphosphate-inhibited form as Protein Data Bank file 3H6M: [2] or 1SNC: [3]. As seen in the ribbon diagram above, the nuclease molecule has 3 long alpha helices and a 5-stranded, barrel-shaped beta sheet, in an arrangement known as the OB-fold (for oligonucleotide-binding fold) as classified in the SCOP database.
Applications
- Hydrolysis of nucleic acids in crude cell-free extracts.
- Sequencing of RNA.
- Preparation of rabbit reticulocyte lysates.
- Studies of chromatin structure.
- Removal of nucleic acids from laboratory protein preparations allowing for protein folding and structure-function studies.
- Research on the mechanisms of protein folding.
References
- ^ Heins JN, Suriano JR, Taniuchi H, Anfinsen CB (1967). "Characterization of a nuclease produced by Staphylococcus aureus". J. Biol. Chem. 242 (5): 1016–20. PMID 6020427.
- ^ Cusumano CL, Taniuchi H, Anfinsen CB (1968). "Staphylococcal nuclease (Foggi strain). I. Order of cyanogen bromide fragments and a "fourth" histidine residue". J. Biol. Chem. 243 (18): 4769–77. PMID 5687719.
- ^ Arnone A, Bier J, et al. (1971). "A High Resolution Structure of an Inhibitor Complex of the Extracellular Nuclease of Staphylococcus aureus: I. Experimental Procedures and Chain Tracing". J. Biol. Chem. 246: 2303–2316.
- http://www.thermoscientificbio.com/dna-and-rna-modifying-enzymes/micrococcal-nuclease/
- http://www.worthington-biochem.com/NFCP/default.html
- http://www.thermoscientificbio.com/uploadedFiles/Resources/en0181-usa-msds.pdf - A material and safety data sheet for the product
- http://www.thermoscientificbio.com/uploadedFiles/Resources/en018-product-information.pdf - A Product Information sheet
External links
- Micrococcal Nuclease at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.1.31.1
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Hydrolase: esterases (EC 3.1)
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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
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| 3.1.2: Thioesterase |
- Palmitoyl protein thioesterase
- Ubiquitin carboxy-terminal hydrolase L1
- 4-hydroxybenzoyl-CoA thioesterase
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| 3.1.3: Phosphatase |
- Alkaline phosphatase
- Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
- Nucleotidase
- Glucose 6-phosphatase
- Fructose 1,6-bisphosphatase
- Protein phosphatase
- OCRL
- Pyruvate dehydrogenase phosphatase
- Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
- PTEN
- Phytase
- Inositol-phosphate phosphatase
- Protein phosphatase: Protein tyrosine phosphatase
- Protein serine/threonine phosphatase
- Dual-specificity phosphatase
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| 3.1.4: Phosphodiesterase |
- Autotaxin
- Phospholipase
- Sphingomyelin phosphodiesterase
- PDE1
- PDE2
- PDE3
- PDE4A/PDE4B
- PDE5
- Lecithinase (Clostridium perfringens alpha toxin)
- Cyclic nucleotide phosphodiesterase
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| 3.1.6: Sulfatase |
- arylsulfatase
- Arylsulfatase A
- Arylsulfatase B
- Arylsulfatase E
- Steroid sulfatase
- Galactosamine-6 sulfatase
- Iduronate-2-sulfatase
- N-acetylglucosamine-6-sulfatase
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Nuclease (includes
deoxyribonuclease and
ribonuclease) |
| 3.1.11-16: Exonuclease |
| Exodeoxyribonuclease |
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| Exoribonuclease |
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| 3.1.21-31: Endonuclease |
| Endodeoxyribonuclease |
- Deoxyribonuclease I
- Deoxyribonuclease II
- Deoxyribonuclease IV
- Restriction enzyme
- UvrABC endonuclease
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| Endoribonuclease |
- RNase III
- RNase H
- RNase P
- RNase A
- RNase T1
- RNA-induced silencing complex
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| either deoxy- or ribo- |
- Aspergillus nuclease S1
- Micrococcal nuclease
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Enzymes
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| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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UpToDate Contents
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English Journal
- Chromatin Accessibility at a STAT3 Target Site Is Altered Prior to Astrocyte Differentiation.
- Urayama S, Semi K, Sanosaka T, Hori Y, Namihira M, Kohyama J, Takizawa T, Nakashima K.SourceLaboratory of Molecular Neuroscience, Graduate School of Biological Sciences, Nara Institute of Science and Technology.
- Cell structure and function.Cell Struct Funct.2013 Apr 18;38(1):55-66. Epub 2013 Feb 26.
- DNA demethylation of astrocyte-specific gene promoters and STAT3 activation in neural precursor cells (NPCs) are essential for astrogliogenesis in the developing brain. To date, it remains unclear whether DNA methylation is the sole epigenetic determinant responsible for suppressing astrocyte-specif
- PMID 23439558
- An ultra-high sensitive platform for fluorescence detection of micrococcal nuclease based on graphene oxide.
- He Y, Xiong LH, Xing XJ, Tang HW, Pang DW.SourceCollege of Chemistry and Molecular Sciences, Research Center for Nanobiology and Nanomedicine-MOE 985 Innovative Platform, Wuhan Institute of Biotechnology, and State Key Laboratory of Virology, Wuhan University, Wuhan 430072, China.
- Biosensors & bioelectronics.Biosens Bioelectron.2013 Apr 15;42:467-73. doi: 10.1016/j.bios.2012.10.045. Epub 2012 Oct 23.
- Micrococcal nuclease (MNase) is the extracellular nuclease of Staphylococcus aureus (S. aureus). It preferentially digests single-stranded nucleic acids. The existence of MNase can be the standard to identify S. aureus and the content of MNase can be used to evaluate the pathogenicity of S. aureus.
- PMID 23238320
- Methylation of SUV39H1 by SET7/9 results in heterochromatin relaxation and genome instability.
- Wang D, Zhou J, Liu X, Lu D, Shen C, Du Y, Wei FZ, Song B, Lu X, Yu Y, Wang L, Zhao Y, Wang H, Yang Y, Akiyama Y, Zhang H, Zhu WG.SourceKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Department of Biochemistry and Molecular Biology, and Department of Anatomy, Histology, and Embryology, Peking University Health Science Center, Beijing 100191, China.
- Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2013 Apr 2;110(14):5516-21. doi: 10.1073/pnas.1216596110. Epub 2013 Mar 18.
- Suppressor of variegation 3-9 homolog 1 (SUV39H1), a histone methyltransferase, catalyzes histone 3 lysine 9 trimethylation and is involved in heterochromatin organization and genome stability. However, the mechanism for regulation of the enzymatic activity of SUV39H1 in cancer cells is not yet well
- PMID 23509280
Japanese Journal
- GTS1 Induction Causes Derepression of Tup1-Cyc8-Repressing Genes and Chromatin Remodeling through the Interaction of Gts1p with Cyc8p
- Sanada Mitsuaki,Kuroda Kouichi,Ueda Mitsuyoshi
- Bioscience, biotechnology, and biochemistry 75(4), 740-747, 2011-04-23
- … GTS1 induction caused chromatin remodeling at the FLO1 promoter in a SWI/SNF-dependent manner on micrococcal nuclease accessibility assay. …
- NAID 10028271704
- Intermediate structure between chromatin fibers and chromosome revealed by mechanical stretching and SPM measurement
- Ikeda Kensuke,Mizutani Takeomi,Hoshi Osamu,Ushiki Tatsuo,Haga Hisashi,Kawabata Kazushige
- Biochemical and Biophysical Research Communications 400(1), 181-186, 2010-09-10
- … Furthermore, after micrococcal nuclease and trypsin treatments, the fibers were found to be mechanically supported by proteins. …
- NAID 120002473469
- Radiation-induced XRCC4 Association with Chromatin DNA Analyzed by Biochemical Fractionation
- Kamdar Radhika Pankaj,Matsumoto Yoshihisa
- Journal of radiation research 51(3), 303-313, 2010-05-16
- … This form of XRCC4 was liberated by micrococcal nuclease treatment, indicating that it had been tethered to chromatin DNA. …
- NAID 10026471164
Related Links
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- Categories: Nuclease Products Applications: ChIP Product Information FAQs Other Tools & Resources Related Products Tech Tips Description Advantages and Features Properties and Usage Quality Control Description Micrococcal ...
Related Pictures
★リンクテーブル★
[★]
- 英
- micrococcal nuclease
- 関
- ミクロコッカス、ミクロコッカス属
[★]
- 関
- micrococci、Micrococcus
[★]
ヌクレアーゼ、核酸分解酵素