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- ribonuclease T1
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/04/03 09:37:55」(JST)
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| Ribonuclease T1 |
| Identifiers |
| EC number |
3.1.27.3 |
| CAS number |
9026-12-4 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Gene Ontology |
AmiGO / EGO |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
|
| Ribonuclease T1 |
|
| Ribonuclease T1 from Aspergillus oryzae.[1] |
| Identifiers |
| Symbol |
? |
| PDB |
1YGW |
| UniProt |
P00651 |
| Other data |
| EC number |
3.1.27.3 |
Ribonuclease T1 (sometimes abbreviated RNase T1) is a fungal endonuclease that cleaves single-stranded RNA after guanine residues, i.e., on their 3' end; the most commonly studied form of this enzyme is the version found in the mold Aspergillus oryzae. Owing to its specificity for guanine, RNase T1 is often used to digest denatured RNA prior to sequencing. Similar to other ribonucleases such as barnase and RNase A, ribonuclease T1 has been popular for folding studies.[2]
Structurally, ribonuclease T1 is a small α+β protein (104 amino acids) with a four-stranded, antiparallel beta sheet covering a long alpha helix (almost five turns). RNase T1 has two disulfide bonds, Cys2-Cys10 and Cys6-Cys103, of which the latter contributes more to its folding stability;[3] complete reduction of both disulfides usually unfolds the protein, although its folding can be rescued with high salt concentrations.[4]
RNase T1 also has four prolines, two of which (Pro39 and Pro55) have cis isomers of their X-Pro peptide bonds. Nonnative isomers of these prolines can retard conformational folding dramatically,[5] folding on a characteristic time scale of 7,000 seconds (almost two hours) at 10°C and pH 5.[6]
References
- ^ PDB 1ygw; Pfeiffer S, Karimi-Nejad Y, Rüterjans H (February 1997). "Limits of NMR structure determination using variable target function calculations: ribonuclease T1, a case study". J. Mol. Biol. 266 (2): 400–23. doi:10.1006/jmbi.1996.0784. PMID 9047372.
- ^ Pace, CN; Heinemann U, Hahn U, Saenger W (1991). "Ribonuclease T1: Structure, Function, and Stability". Angewandte Cheni, International Edition 30 (4): 343–360. doi:10.1002/anie.199103433.
- ^ Pace, CN; Grimsley GR, Thomson JA, Barnett BJ (1988). "Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds". Journal of Biological Chemistry 263 (24): 11820–11825. PMID 2457027.
- ^ Oobatake, M; Takahashi S, Ooi T (1979). "Conformational stability of ribonuclease T1. II. Salt-induced renaturation". Journal of Biochemistry (Tokyo) 86: 65–70.
- ^ Mayr, LM; Odefey CO, Schutkowski M, Schmid FX (1996). "Kinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique". Biochemistry 35 (17): 5550–5561. doi:10.1021/bi953035y. PMID 8611546.
- ^ Mullins, LS; Pace CN and Raushel FM (1997). "Conformational stability of ribonuclease T1 measured by hydrogen-deuterium exchange". Protein Science 6 (7): 1387–1395. doi:10.1002/pro.5560060702. PMC 2143755. PMID 9232639.
External links
- Ribonuclease T1 at the US National Library of Medicine Medical Subject Headings (MeSH)
|
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
- 2.7.10
- 2.7.11-12
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
UpToDate Contents
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English Journal
- Involvement of loop 5 lysine residues and the N-terminal β-hairpin of the ribotoxin hirsutellin A on its insecticidal activity.
- Olombrada M, García-Ortega L, Lacadena J, Oñaderra M, Gavilanes JG, Martínez-Del-Pozo Á.
- Biological chemistry.Biol Chem.2016 Jan 1;397(2):135-45. doi: 10.1515/hsz-2015-0261.
- Ribotoxins are cytotoxic members of the family of fungal extracellular ribonucleases best represented by RNase T1. They share a high degree of sequence identity and a common structural fold, including the geometric arrangement of their active sites. However, ribotoxins are larger, with a well-define
- PMID 26584355
- The RNA Stem-Loop to G-Quadruplex Equilibrium Controls Mature MicroRNA Production inside the Cell.
- Pandey S1,2, Agarwala P1,2, Jayaraj GG1,2, Gargallo R3, Maiti S1,2,4.
- Biochemistry.Biochemistry.2015 Dec 8;54(48):7067-78. doi: 10.1021/acs.biochem.5b00574. Epub 2015 Nov 19.
- The biological role of the existence of overlapping structures in RNA is possible yet remains very unexplored. G-Rich tracts of RNA form G-quadruplexes, while GC-rich sequences prefer stem-loop structures. The equilibrium between alternate structures within RNA may occur and influence its functional
- PMID 26554903
- Detection of RNA nucleoside modifications with the uridine-specific ribonuclease MC1 from Momordica charantia.
- Addepalli B1, Lesner NP2, Limbach PA1.
- RNA (New York, N.Y.).RNA.2015 Oct;21(10):1746-56. doi: 10.1261/rna.052472.115. Epub 2015 Jul 28.
- A codon-optimized recombinant ribonuclease, MC1 is characterized for its uridine-specific cleavage ability to map nucleoside modifications in RNA. The published MC1 amino acid sequence, as noted in a previous study, was used as a template to construct a synthetic gene with a natural codon bias favor
- PMID 26221047
Japanese Journal
- X-Ray Crystallographic Structure of RNase Po1 That Exhibits Anti-tumor Activity
- The Inhibition of Human Tumor Cell Proliferation by RNase Pol, a Member of the RNase T1 Family, from Pleurotus ostreatus
- Bioscience, biotechnology, and biochemistry 77(7), 1486-1491, 2013-07-23
- NAID 10031190457
- Structure and function studies on enzymes with a catalytic carboxyl group(s) : from ribonuclease T₁ to carboxyl peptidases
Related Links
- RNAマッピングおよび構造研究。エア・ブラウン ライフサイエンス ... アプリケーション RNAマッピングおよび構造研究 DNA調製物からRNAを除去 RNAプロテクションアッセイ Ribonuclease T1(RNase T1)はRNAまたは脱アミノ化されたRNAを ...
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Related Pictures
★リンクテーブル★
[★]
リボヌクレアーゼT1
- 関
- RNase T1
[★]
- 英
- ribonuclease T1、RNase T1
[★]