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the 20th letter of the Roman alphabet (同)t

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tritiumの化学記号

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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 (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)

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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

Biological and Pharmaceutical Bulletin 37(6), 968-978, 2014
NAID 130004147340

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

Proceedings of the Japan Academy, Series B 89(6), 201-225, 2013
NAID 130003365117

「ribonuclease T1」

Ribonuclease T1
	Ribonuclease T1 from Aspergillus oryzae.
Identifiers
Symbol	?
PDB	1YGW
UniProt	P00651
Other data
EC number	3.1.27.3

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
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PMC	articles
PubMed	articles
NCBI	proteins