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Titolo:
A NOVEL GTPASE-ACTIVATING PROTEIN FOR R-RAS
Autore:
YAMAMOTO T; MATSUI T; NAKAFUKU M; IWAMATSU A; KAIBUCHI K;
Indirizzi:
NARA INST SCI & TECHNOL,DIV SIGNAL TRANSDUCT IKOMA NARA 63001 JAPAN NARA INST SCI & TECHNOL,DIV SIGNAL TRANSDUCT IKOMA NARA 63001 JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL YOKOHAMA KANAGAWA 236 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 51, volume: 270, anno: 1995,
pagine: 30557 - 30561
SICI:
0021-9258(1995)270:51<30557:ANGPFR>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-CLONING; SACCHAROMYCES-CEREVISIAE; EXCHANGE PROTEIN; DOMAIN; GENE; BINDING; P21; IDENTIFICATION; KINASE; CDNA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
T. Yamamoto et al., "A NOVEL GTPASE-ACTIVATING PROTEIN FOR R-RAS", The Journal of biological chemistry, 270(51), 1995, pp. 30557-30561

Abstract

R-Ras, belonging to the Pas small GTP-binding protein superfamily, has been implicated in regulation of various cell functions such as geneexpression, cell proliferation, and apoptotic cell death. In the present study, we purified an R-Ras-interacting protein with molecular mass of about 98 kDa (p98) from bovine brain cytosol by glutathione S-transferase (GST)-R-Ras affinity column chromatography. This protein bound to GTP gamma S (guanosine 5'-(3-O-thio)triphosphate, a nonhydrolyzable GTP analog). R-Ras but not to GDP . R-Ras, GTP gamma S . R-Ras witha mutation in the effector domain (R-Ras(A64)), GTP gamma S . Ha-Ras,or GTP gamma S . RalA. We obtained a cDNA encoding p98 on the basis of its partial amino acid sequences, The predicted protein consists of 834 amino acids whose calculated mass, 95,384 Da, is close to the apparent molecular mass of p98. The amino acid sequence shows a high degree of sequence similarity to the entire sequence of Gap1(m), one of theGTPase-activating proteins (GAP) for Ha-Ras. A recombinant protein consisting of the GAP-related domain of p98 fused to maltose-binding protein stimulated GTPase activity of R-Ras, and showed a weak effect on that of Ha-Ras but not that of Rap1 or Rho. These results clearly indicate that p98 is a novel GAP for R-Ras. Thus, we designated this protein as R-Ras GAP.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 01:22:55