scholarly journals Spatial regulation of the guanine nucleotide exchange factor Lte1 in Saccharomyces cerevisiae

2002 ◽  
Vol 115 (24) ◽  
pp. 4977-4991 ◽  
Author(s):  
S. Jensen
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Guanine Nucleotide Exchange Factor ◽  
Guanine Nucleotide ◽  
Nucleotide Exchange ◽  
Exchange Factor ◽  
Spatial Regulation ◽  
Guanine Nucleotide Exchange ◽  
Nucleotide Exchange Factor

scholarly journals SDC25, a dispensable Ras guanine nucleotide exchange factor of Saccharomyces cerevisiae differs from CDC25 by its regulation.

1996 ◽  
Vol 7 (4) ◽  
pp. 529-539 ◽  
Author(s):  
E Boy-Marcotte ◽  
P Ikonomi ◽  
M Jacquet
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Carbon Source ◽  
Transcriptional Control ◽  
Carbon Sources ◽  
Guanine Nucleotide Exchange Factor ◽  
Guanine Nucleotide ◽  
Nucleotide Exchange ◽  
Exchange Factor ◽  
Guanine Nucleotide Exchange ◽  
Nucleotide Exchange Factor

The SDC25 gene of Saccharomyces cerevisiae is homologous to CDC25. Its 3' domain encodes a guanine nucleotide exchange factor (GEF) for Ras. Nevertheless, the GEF encoded by CDC24 is determinant for the Ras/cAMP pathway activation in growth. We demonstrate that the SDC25 gene product is a functional GEF for Ras: the complete SDC25 gene functionally replaces CDC25 when overexpressed or when transcribed under CDC25 transcriptional control at the CDC25 locus. Chimeric proteins between Sdc25p and Cdc25p are also functional GEFs for Ras. We also show that the two genes are differentially regulated: SDC25 is not transcribed at a detectable level in growth conditions when glucose is the carbon source. It is transcribed at the end of growth when nutrients are depleted and in cells grown on nonfermentable carbon sources. In contrast, CDC25 accumulation is slightly reduced when glucose is replaced by a nonfermentable carbon source.

Saccharomyces cerevisiae CDC25 [1028-1589] is a guanine nucleotide exchange factor for mammalian ras proteins and is ongenic in HIH3T3 cells

1992 ◽  
Vol 76 (2) ◽  
pp. 229-229
Author(s):  
Marie-Christine Chevallier-Multon ◽  
Fabien Schweighoffer ◽  
Isabelle Barlat ◽  
Nicole Baudouy ◽  
Isabelle Fath ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Guanine Nucleotide Exchange Factor ◽  
Guanine Nucleotide ◽  
Nucleotide Exchange ◽  
Ras Proteins ◽  
Exchange Factor ◽  
Guanine Nucleotide Exchange ◽  
Nucleotide Exchange Factor

scholarly journals Characterization of Synthetic-Lethal Mutants Reveals a Role for the Saccharomyces cerevisiae Guanine-Nucleotide Exchange Factor Cdc24p in Vacuole Function and Na+ Tolerance

Genetics ◽  
1997 ◽  
Vol 147 (1) ◽  
pp. 43-55 ◽  
Author(s):  
William H White ◽  
Douglas I Johnson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Polarity ◽  
Synthetic Lethality ◽  
Guanine Nucleotide Exchange Factor ◽  
Guanine Nucleotide ◽  
Nucleotide Exchange ◽  
Synthetic Lethal ◽  
Exchange Factor ◽  
Guanine Nucleotide Exchange ◽  
Nucleotide Exchange Factor

Abstract Cdc24p is the guanine-nucleotide exchange factor for the Cdc42p GTPase, which controls cell polarity in Saccharomyces cerevisiae. To identify new genes that may affect cell polarity, we characterized six UV-induced csl (CDC24  synthetic-lethal) mutants that exhibited synthetic-lethality with cdc24-4ts at 23°. Five mutants were not complemented by plasmid-borne CDC42, RSRI, BUD5, BEM1, BEM2, BEM3 or CLA4 genes, which are known to play a role in cell polarity. The csl3 mutant displayed phenotypes similar to those observed with calcium-sensitive, Pet−  vma mutants defective in vacuole function. CSL5 was allelic to VMA5, the vacuolar H+-ATPase subunit C, and one third of cs15 cdc24-4ts cells were elongated or had misshapen buds. A cdc24-4ts Δvma5::LEU2 double mutant did not exhibit synthetic lethality, suggesting that the csl5/vma5 cdc24-4ts synthetic-lethality was not simply due to altered vacuole function. The cdc24-4ts mutant, like Δvma5::LEU2 and cs13 mutants, was sensitive to high levels of Ca2+ as well as Na+ in the growth media, which did not appear to be a result of a fragile cell wall because the phenotypes were not remedied by 1 m sorbitol. Our results indicated that Cdc24p was required in one V-ATPase mutant and another mutant affecting vacuole morphology, and also implicated Cdc24p in Na+ tolerance.

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