Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae

被引:243
作者
Kohno, H
Tanaka, K
Mino, A
Umikawa, M
Imamura, H
Fujiwara, T
Fujita, Y
Hotta, K
Qadota, H
Watanabe, T
Ohya, Y
Takai, Y
机构
[1] OSAKA UNIV, SCH MED, DEPT MOL BIOL & BIOCHEM, SUITA, OSAKA 565, JAPAN
[2] UNIV TOKYO, GRAD SCH SCI, DEPT BIOL SCI, BUNKYO KU, TOKYO 113, JAPAN
[3] NIPPON ROCHE RES CTR, DEPT MYCOL, KAMAKURA, KANAGAWA 247, JAPAN
关键词
actin cytoskeleton; Rho target; S-cerevisiae;
D O I
10.1002/j.1460-2075.1996.tb00994.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The RHO1 gene encodes a homolog of mammalian RhoA small GTP binding protein in the yeast Saccharomyces cerevisiae, Rho1p is localized at the growth sites, including the bud tip and the cytokinesis site, and is required for bud formation, We have recently shown that Pkc1p, a yeast homolog of mammalian protein kinase C, and glucan synthase are targets of Rho1p, Using the two-hybrid screening system, we cloned a gene encoding a protein which interacted with the GTP-bound form of Rho1p, This gene was identified as BN11, known to be implicated in cytokinesis or establishment of cell polarity in S.cerevisiae. Bni1p shares homologous domains (FH1 and FH2 domains) with proteins involved in cytokinesis or establishment of cell polarity, including formin of mouse, capu and dia of Drosophila and FigA of Aspergillus. A temperature-sensitive mutation in which the RHO1 gene was replaced by the mammalian RhoA gene showed a synthetically lethal interaction with the bni1 mutation and the RhoA bni1 mutant accumulated cells with a deficiency in cytokinesis, Furthermore, this synthetic lethality was caused by the incapability of RhoA to activate Pkc1p, but not glucan synthase, These results suggest that Rho1p regulates cytoskeletal reorganization at least through Bni1p and Pkc1p.
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收藏
页码:6060 / 6068
页数:9
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