リボヌクレアーゼIII
WordNet
- the 9th letter of the Roman alphabet (同)i
- a transferase that catalyzes the hydrolysis of ribonucleic acid (同)ribonucleinase, RNase
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Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/01/17 12:44:45」(JST)
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| Ribonuclease III domain |
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Ribonuclease III structure interacting with double stranded RNA.
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| Identifiers |
| Symbol |
RNase_III |
| Pfam |
PF00636 |
| InterPro |
IPR000999 |
| PROSITE |
PDOC00448 |
| SCOP |
1jfz |
| SUPERFAMILY |
1jfz |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
RNase III is a type of ribonuclease that specifically binds to and cleaves double-stranded RNA (dsRNA).[1] There are four subdivisions, known as Class 1, 2, 3, and 4.
Prokaryotic ribonuclease III (EC 3.1.26.3) (gene rnc)[2] is an enzyme that digests double-stranded RNA. It is involved in the processing of ribosomal RNA precursors and of some mRNAs.
- Class 1 RNases III are largely found in bacteria, bacteriophage, and some fungi. Among the RNases III in the class are the rnc from E. coli, Pac1p from S. pombe, and Rnt1p from S. cerevisiae. Class 1 RNases III process precursors to ribosomal RNA, and in the case of fungi, process precursors to small nuclear RNA (snRNA) and small nucleolar RNA (snoRNA).
- Class 2 RNases III include the Drosha family of enzymes known to function in maturation of precursors to miRNA.[3]
- Class 3 RNases III include the Dicer family of enzymes known to function in RNA interference (RNAi).[4]
- Class 4 RNases III called Mini-III are homodimeric enzymes and consist solely of the RNase III domains.[5]
Human proteins containing this domain
DICER1; MRPL44; RNASEN;
See also
External links
- RNase III at the US National Library of Medicine Medical Subject Headings (MeSH)
- EC 3.1.26.3
References
- ^ Lamontagne, B.; Larose, S.; Boulanger, J.; Elela, S. (2001). "The RNase III family: A conserved structure and expanding functions in eukaryotic dsRNA metabolism". Current issues in molecular biology 3 (4): 71–78. PMID 11719970.
- ^ Nashimoto H, Uchida H (1985). "DNA sequencing of the Escherichia coli ribonuclease III gene and its mutations". Mol. Gen. Genet. 201 (1): 25–29. doi:10.1007/bf00397981. PMID 3903434.
- ^ Filippov V, Solovyev V, Filippova M, Gill SS (Mar 2000). "A novel type of RNase III family proteins in eukaryotes". Gene 245 (1): 213–221. doi:10.1016/S0378-1119(99)00571-5. PMID 10713462.
- ^ Bernstein E, Caudy AA, Hammond SM, Hannon GJ (2001). "Role for a bidentate ribonuclease in the initiation step of RNA interference". Nature 409 (6818): 363–6. doi:10.1038/35053110. PMID 11201747.
- ^ Glow, D.; Pianka, D.; Sulej, A. A.; Kozlowski, Lukasz P.; Czarnecka, J.; Chojnowski, G.; Skowronek, K. J.; Bujnicki, J. M. (2015). "Sequence-specific cleavage of dsRNA by Mini-III RNase". Nucleic Acids Research 43 (5): 2864–2873. doi:10.1093/nar/gkv009. ISSN 0305-1048. PMID 25634891.
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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
|
|
| 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
- 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
|
|
| 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 |
|
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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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- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 9
- 10
- 11
- 12
- 13
- 14
- 15-99
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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This article incorporates text from the public domain Pfam and InterPro IPR000999
UpToDate Contents
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English Journal
- Molecular recognition of mRNA 5' cap by 3' poly(A)-specific ribonuclease (PARN) differs from interactions known for other cap-binding proteins.
- Niedzwiecka A1, Nilsson P2, Worch R3, Stepinski J4, Darzynkiewicz E5, Virtanen A2.
- Biochimica et biophysica acta.Biochim Biophys Acta.2016 Apr;1864(4):331-45. doi: 10.1016/j.bbapap.2016.01.002. Epub 2016 Jan 6.
- The mRNA 5' cap structure plays a pivotal role in coordination of eukaryotic translation and mRNA degradation. Poly(A)-specific ribonuclease (PARN) is a dimeric exoribonuclease that efficiently degrades mRNA 3' poly(A) tails while also simultaneously interacting with the mRNA 5' cap. The cap binding
- PMID 26772900
- Characterization of ribonuclease III from Brucella.
- Wu CX1, Xu XJ1, Zheng K1, Liu F1, Yang XD1, Chen CF2, Chen HC1, Liu ZF3.
- Gene.Gene.2016 Apr 1;579(2):183-92. doi: 10.1016/j.gene.2015.12.068. Epub 2016 Jan 8.
- Bacterial ribonuclease III (RNase III) is a highly conserved endonuclease, which plays pivotal roles in RNA maturation and decay pathways by cleaving double-stranded structure of RNAs. Here we cloned rncS gene from the genomic DNA of Brucella melitensis, and analyzed the cleavage properties of RNase
- PMID 26778206
- MicroRNA Biogenesis and Hedgehog-Patched Signaling Cooperate to Regulate an Important Developmental Transition in Granule Cell Development.
- Constantin L1, Constantin M2, Wainwright BJ3.
- Genetics.Genetics.2016 Mar;202(3):1105-18. doi: 10.1534/genetics.115.184176. Epub 2016 Jan 15.
- The Dicer1, Dcr-1 homolog (Drosophila) gene encodes a type III ribonuclease required for the canonical maturation and functioning of microRNAs (miRNAs). Subsets of miRNAs are known to regulate normal cerebellar granule cell development, in addition to the growth and progression of medulloblastoma, a
- PMID 26773048
Japanese Journal
- Inhibitiory effects of gold(III) ions on ribonuclease and deoxyribonuclease
- 食道扁平上皮癌におけるRNASEN (ribonuclease III, nuclear)の発現と臨床病理学的意義
- 杉戸 伸好,桑原 義之,木村 昌弘,三井 章,石黒 秀行,安藤 拓也,呉原 裕樹,友田 圭介,森 亮太,高嶋 伸宏,藤井 義敬
- 日本外科学会雑誌 107(臨時増刊号_2), 248, 2006-03-05
- NAID 110004710953
- RNAiを用いた遺伝子ノックダウン法の基本テクニック(ショートコース10)
Related Links
- RNase III an enzyme catalyzing endonucleolytic cleavage of double-stranded RNA, yielding 5'-phosphomonoesters; preference for multimeric tRNA precursors. ... The primary miRNAs are cleaved by ribonuclease III Drosha and the ...
- "Ribonuclease III" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are ... Thivierge C, Makil N, Flamand M, Vasale JJ, Mello CC, Wohlschlegel J ...
★リンクテーブル★
[★]
- 英
- ribonuclease III, RNaseIII, RNase III
- 同
- RNアーゼIII
[★]
[★]
[★]
リボヌクレアーゼ