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Titolo:
BYR4 AND CDC16 FORM A 2-COMPONENT GTPASE-ACTIVATING PROTEIN FOR THE SPG1 GTPASE THAT CONTROLS SEPTATION IN FISSION YEAST
Autore:
FURGE KA; WONG K; ARMSTRONG J; BALASUBRAMANIAN M; ALBRIGHT CF;
Indirizzi:
VANDERBILT UNIV,DEPT BIOCHEM,SCH MED NASHVILLE TN 37232 VANDERBILT UNIV,DEPT BIOCHEM,SCH MED NASHVILLE TN 37232 NATL UNIV SINGAPORE,INST MOL AGROBIOL SINGAPORE 117604 SINGAPORE UNIV SUSSEX,SCH BIOL SCI BRIGHTON BN1 9QG E SUSSEX ENGLAND
Titolo Testata:
Current biology
fascicolo: 17, volume: 8, anno: 1998,
pagine: 947 - 954
SICI:
0960-9822(1998)8:17<947:BACFA2>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
SCHIZOSACCHAROMYCES-POMBE; SEPTUM FORMATION; QUANTITATIVE-ANALYSIS; BINDING DOMAIN; HUMAN RAF-1; RAS; RANBP1; KINASE; PURIFICATION; CYTOKINESIS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
K.A. Furge et al., "BYR4 AND CDC16 FORM A 2-COMPONENT GTPASE-ACTIVATING PROTEIN FOR THE SPG1 GTPASE THAT CONTROLS SEPTATION IN FISSION YEAST", Current biology, 8(17), 1998, pp. 947-954

Abstract

Background: Spatial and temporal control of cytokinesis ensures the accurate transmission of genetic material and the correct development of multicellular organisms. An excellent model system in which to studycytokinesis is Schizosaccharomyces pombe because there are similarities between cytokinesis in S. pombe and mammals and because genes involved in S. pombe cytokinesis have been characterized. In particular, formation of the septum is positively regulated by the Spg1 GTPase and its effector, the Cdc7 kinase. Septation is negatively regulated by Cdc16, a protein similar to GTPase-activating proteins (GAPs) for Ypt GTPases, and by Byr4, a protein of unknown biochemical function. This study investigates the relationship between Byr4, Cdc16, and Spg1. Results: Genetic interactions were observed between byr4, cdc16, and spg1 mutants. Byrd; bound to Cdc16 and Spg1 in yeast two-hybrid assays and incoprecipitations in vitro and in yeast. Byr4 inhibited the dissociation and hydrolysis of GTP bound to Spg1, but when Byr4 and Cdc16 were combined together they displayed Spg1 GAP activity in vitro; Cdc16 alone had no detectable GAP activity. The binding of Byr4 to Spg1 and the Byr4-Cdc16 Spg1 GAP activity were specific because Byr4 and Cdc16 did not bind to or affect the GTPase activities of the seven known S. pombe Ypt family GTPases. Conclusions: Byr4 and Cdc16 form a two-componentGAP for the Spg1 GTPase, Byr4 and Cdc16 appear to negatively regulateseptation in S. pombe by modulating the nucleotide state of Spg1 possibly in a spatially or temporally controlled manner.

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Documento generato il 31/03/20 alle ore 19:43:26