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Titolo:
Proteolytic fragmentation of polypeptide release factor 1 of Thermus thermophilus and crystallization of the stable fragments
Autore:
Tin, OF; Rykunova, AI; Muranova, TA; Toyoda, T; Itoa, K; Suzuki, T; Watanabe, K; Garber, MB; Nakamura, Y;
Indirizzi:
Univ Tokyo, Inst Med Sci, Dept Tumor Biol, Minato Ku, Tokyo 108, Japan Univ Tokyo Tokyo Japan 108 Dept Tumor Biol, Minato Ku, Tokyo 108, Japan Russian Acad Sci, Inst Prot Res, Pushchino 142292, Moscow Region, Russia Russian Acad Sci Pushchino Moscow Region Russia 142292 cow Region, Russia Russian Acad Sci, Branch Shemyakin, Pushchino 142292, Moscow Region, Russia Russian Acad Sci Pushchino Moscow Region Russia 142292 cow Region, Russia Russian Acad Sci, Ovchinnikov Inst Bioorgan Chem, Pushchino 142292, MoscowRegion, Russia Russian Acad Sci Pushchino Moscow Region Russia 142292 scowRegion, Russia Univ Tokyo, BRAIN Basic Res Innovat Biosci Program, Biooriented Technol Res Adv Inst, Minato Ku, Tokyo 108, Japan Univ Tokyo Tokyo Japan 108 nol Res Adv Inst, Minato Ku, Tokyo 108, Japan Univ Tokyo, Grad Sch Frontier Sci, Dept Integrated Biosci, Bunkyo Ku, Tokyo 1138656, Japan Univ Tokyo Tokyo Japan 1138656 d Biosci, Bunkyo Ku, Tokyo 1138656, Japan
Titolo Testata:
BIOCHIMIE
fascicolo: 8, volume: 82, anno: 2000,
pagine: 765 - 772
SICI:
0300-9084(200008)82:8<765:PFOPRF>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELONGATION-FACTOR-G; CRYSTAL-STRUCTURE; PROTEINS; DNA;
Keywords:
translation termination; polypeptide release factor 1; limited proteolysis; crystallization;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Nakamura, Y Univ Tokyo, Inst Med Sci, Dept Tumor Biol, Minato Ku, 4-6-1 Shirokanedai, Tokyo 108, Japan Univ Tokyo 4-6-1 Shirokanedai Tokyo Japan 108okyo 108, Japan
Citazione:
O.F. Tin et al., "Proteolytic fragmentation of polypeptide release factor 1 of Thermus thermophilus and crystallization of the stable fragments", BIOCHIMIE, 82(8), 2000, pp. 765-772

Abstract

Polypeptide release factor one from Thermus thermophilus, ttRF1, was purified and subjected to crystallization. Thin crystalline needles were obtained but their quality was not satisfactory for X-ray diffraction. Stable fragments of ttRF1 suitable for crystallization were screened by limited proteolysis. Three major fragments were produced by thermolysinolysis and analyzed by N-terminal sequencing and electrospray mass spectrometry. They were N-terminal fragments generated by proteolysis at amino acid positions 211, 231 and 292. The corresponding recombinant polypeptides, ttRF1(211), ttRF1(231) and ttRF1(292), were overproduced and subjected to crystallization Of these polypeptides, ttRF1292 gave rise to crystals that belong to P3(1) (or P3(2)) space group with unit cell parameters a = b = 64.5 Angstrom, c = 86.6Angstrom and diffract up to 7 Angstrom resolution. (C) 2000 Societe francaise de biochimie et biologie moleculaire / Editions scientifiques et medicales Elsevier SAS.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 15:26:51