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Titolo:
Amino acids and peptides. LVII. Synthetic peptide with a sequence of ribonuclease from Sulfolobus solfataricus, SSR(1-62), does not function as an RNase
Autore:
Joshi, S; Tsuda, Y; Shintomi, N; Kondo, H; Nishiyama, Y; Iwama, M; Ohgi, K; Irie, M; Okada, Y;
Indirizzi:
Kobe Gakuin Univ, Nishi Ku, Kobe, Hyogo 6512180, Japan Kobe Gakuin Univ Kobe Hyogo Japan 6512180 Ku, Kobe, Hyogo 6512180, Japan STAR Biochem, Torrance, CA 90501 USA STAR Biochem Torrance CA USA 90501STAR Biochem, Torrance, CA 90501 USA Seikei Univ, Musashino, Tokyo 1800001, Japan Seikei Univ Musashino Tokyo Japan 1800001 Musashino, Tokyo 1800001, Japan Hoshi Coll Pharm, Shinagawa Ku, Tokyo 1428501, Japan Hoshi Coll Pharm Tokyo Japan 1428501 Shinagawa Ku, Tokyo 1428501, Japan
Titolo Testata:
FEBS LETTERS
fascicolo: 1, volume: 468, anno: 2000,
pagine: 11 - 14
SICI:
0014-5793(20000218)468:1<11:AAAPLS>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
ARCHAEBACTERIUM; ACIDOCALDARIUS; PROTEINS;
Keywords:
circular dichroism spectroscopy; DNA-binding activity; P2; RNase activity; synthetic SSR(1-62); Sulfolobus solfataricus;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
14
Recensione:
Indirizzi per estratti:
Indirizzo: Okada, Y Kobe Gakuin Univ, Nishi Ku, Kobe, Hyogo 6512180, Japan Kobe Gakuin Univ Kobe Hyogo Japan 6512180 , Hyogo 6512180, Japan
Citazione:
S. Joshi et al., "Amino acids and peptides. LVII. Synthetic peptide with a sequence of ribonuclease from Sulfolobus solfataricus, SSR(1-62), does not function as an RNase", FEBS LETTER, 468(1), 2000, pp. 11-14

Abstract

The 62 residue peptide, SSR(1-62), whose sequence corresponds to that of ribonuclease (RNase) from Sulfolobus solfataricus, and its related peptides,SSR(1-22) and SSR(10-62), mere chemically synthesized and their RNase activity and DNA-binding activity were examined. The RNase activity assay usingyeast RNA or tRNA(fMet) as substrate showed that the synthetic peptide SSR(1-62) did not hydrolyze yeast RNA or tRNA(fMet). These data were not consistent with previous reports that both the native peptide isolated from S, solfataricus [Fusi et al, (1993) fur. J. Biochem, 211, 305-311] and the recombinant peptide expressed in Escherichia coli [Fusi et at. (1995) Gene 154,99-103] were able to hydrolyze tRNA(fMet). However, the synthetic SSR(1-62) exhibited DNA-binding activity. In the presence of synthetic SSR(1-62), the cleavage of DNA (plasmid pUCRh2-4) by restriction endonuclease (EcoRI) was not observed, suggesting that synthetic SSR(1-62) bound to DNA protectedDNA from its enzymatic digestion. Neither SSR(1-22) nor SSR(10-62) prevented DNA from being cleaved by a restriction enzyme. These findings strongly suggest the importance of not only the N-terminal region of SSR(1-62) but also the C-terminal region for DNA-binding. Circular dichroism spectroscopy of synthetic SSR(1-62) indicated a beta-sheet conformation, in contrast with synthetic SSR(1-22), which exhibited an unordered conformation. (C) 2000 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/10/20 alle ore 23:11:32