The large N-terminal domain of Cdc25 protein of the yeast Saccharomyces cerevisiae is required for glucose-induced Ras2 activation

被引:11
作者
Paiardi, Chiara [1 ]
Belotti, Fiorella [1 ]
Colombo, Sonia [1 ]
Tisi, Rentata [1 ]
Martegani, Enzo [1 ]
机构
[1] Univ Milano Bicocca, Dept Biotechnol & Biosci, I-20126 Milan, Italy
关键词
Cdc25; RasGTP; cAMP; Saccharomyces cerevisiae;
D O I
10.1111/j.1567-1364.2007.00300.x
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
The Saccharomyces cerevisiae CDC25 gene encodes a guanine nucleotide exchange factor for Ras proteins whose catalytic domain is highly homologous to Ras-guanine nucleotide exchange factors from higher eukaryotes. In this study, glucose-induced Ras activation and cAMP response were investigated in mutants lacking the N-terminal domain of Cdc25 or where the entire CDC25 coding sequence was substituted by an expression cassette for a mammalian guanine nucleotide exchange factor catalytic domain. Our results suggest that an unregulated, low Ras guanine nucleotide exchange factor activity allows a normal glucose-induced cAMP signal that appears to be mediated mainly by the Gpr1/Gpa2 system, but it was not enough to sustain the glucose-induced increase of Ras2-GTP normally observed in a wild-type strain.
引用
收藏
页码:1270 / 1275
页数:6
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