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Gene Review

YLL017W  -  pseudo

Saccharomyces cerevisiae S288c

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High impact information on YLL017W

  • The 3'-terminal part of SCD25, a gene of S. cerevisiae structurally related to CDC25, can suppress the requirement for CDC25 [1].
  • Partially purified preparations of the carboxy-terminal domain of the SCD25 gene product enhanced the exchange rate of guanosine diphosphate (GDP) to guanosine triphosphate (GTP) of pure RAS2 protein by stimulating the release of GDP [1].
  • Mutations of Ha-ras p21 that define important regions for the molecular mechanism of the SDC25 C-domain, a guanine nucleotide dissociation stimulator [2].
  • Using purified RAS proteins, we have found that the SDC25-stimulated conversion of RAS from the GDP-bound inactive state to the GTP-bound active state was severely impaired by amino acid substitutions at positions 80-81 [3].
  • Specifically, SDC25 C domain functions as an exchange factor for cellular Ras proteins in CHO cells [4].

Biological context of YLL017W


Anatomical context of YLL017W


Associations of YLL017W with chemical compounds

  • Guanine Exchange Factor (GEF) activity for Ras proteins has been associated with a conserved domain in Cdc25p, Sdc25p in Saccharomyces cerevisiae and several other proteins recently found in other eukaryotes [11].
  • SDC25, a dispensable Ras guanine nucleotide exchange factor of Saccharomyces cerevisiae differs from CDC25 by its regulation [12].
  • 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 [12].

Physical interactions of YLL017W

  • These results strongly suggest that the residues R80 and N81 are situated in or closely associated with the Ras2p specific site binding Sdc25p [13].

Regulatory relationships of YLL017W

  • In contrast with the C-terminal part, the complete SDC25 gene was found not to suppress the CDC25 gene defect [5].
  • Our results indicate that the SDC25 C-domain activates adenylyl cyclase by rapidly recycling the active RAS2. or RAS1.GTP complex from the respective GDP complex [7].

Other interactions of YLL017W

  • We demonstrate that the GEF domain of Sdc25p is closely related to that of Cdc25p [11].
  • We have introduced single and double amino acid substitutions at positions 80-83 of the RAS2 gene, and we have investigated the interaction of the corresponding proteins with a yeast GDP dissociation stimulator (SDC25 C-domain) [3].
  • We have analyzed the function of this region and the effect of its farnesylation with respect to the action of the GDP/GTP exchange factors (GEFs) Cdc25p and Sdc25p and the target adenylyl cyclase [9].

Analytical, diagnostic and therapeutic context of YLL017W

  • Retention phenomena occurring on gel-filtration chromatography hindered the use of highly purified Sdc25p-C to study the formation of stable complexes with Ras2p [13].


  1. Enhancement of the GDP-GTP exchange of RAS proteins by the carboxyl-terminal domain of SCD25. Créchet, J.B., Poullet, P., Mistou, M.Y., Parmeggiani, A., Camonis, J., Boy-Marcotte, E., Damak, F., Jacquet, M. Science (1990) [Pubmed]
  2. Mutations of Ha-ras p21 that define important regions for the molecular mechanism of the SDC25 C-domain, a guanine nucleotide dissociation stimulator. Mistou, M.Y., Jacquet, E., Poullet, P., Rensland, H., Gideon, P., Schlichting, I., Wittinghofer, A., Parmeggiani, A. EMBO J. (1992) [Pubmed]
  3. RAS residues that are distant from the GDP binding site play a critical role in dissociation factor-stimulated release of GDP. Verrotti, A.C., Créchet, J.B., Di Blasi, F., Seidita, G., Mirisola, M.G., Kavounis, C., Nastopoulos, V., Burderi, E., De Vendittis, E., Parmeggiani, A. EMBO J. (1992) [Pubmed]
  4. The Saccharomyces cerevisiae SDC25 C-domain gene product overcomes the dominant inhibitory activity of Ha-Ras Asn-17. Schweighoffer, F., Cai, H., Chevallier-Multon, M.C., Fath, I., Cooper, G., Tocque, B. Mol. Cell. Biol. (1993) [Pubmed]
  5. SDC25, a CDC25-like gene which contains a RAS-activating domain and is a dispensable gene of Saccharomyces cerevisiae. Damak, F., Boy-Marcotte, E., Le-Roscouet, D., Guilbaud, R., Jacquet, M. Mol. Cell. Biol. (1991) [Pubmed]
  6. The C-terminal part of a gene partially homologous to CDC 25 gene suppresses the cdc25-5 mutation in Saccharomyces cerevisiae. Boy-Marcotte, E., Damak, F., Camonis, J., Garreau, H., Jacquet, M. Gene (1989) [Pubmed]
  7. Properties of the SDC25 C-domain, a GDP to GTP exchange factor of RAS proteins and in vitro modulation of adenylyl cyclase. Créchet, J.B., Poullet, P., Bernardi, A., Fasano, O., Parmeggiani, A. J. Biol. Chem. (1993) [Pubmed]
  8. Interaction between the Saccharomyces cerevisiae CDC25 gene product and mammalian ras. Segal, M., Marbach, I., Engelberg, D., Simchen, G., Levitzki, A. J. Biol. Chem. (1992) [Pubmed]
  9. Analysis of the role of the hypervariable region of yeast Ras2p and its farnesylation in the interaction with exchange factors and adenylyl cyclase. Créchet, J.B., Jacquet, E., Bernardi, A., Parmeggiani, A. J. Biol. Chem. (2000) [Pubmed]
  10. The Saccharomyces cerevisiae gene product SDC25 C-domain functions as an oncoprotein in NIH3T3 cells. Barlat, I., Schweighoffer, F., Chevallier-Multon, M.C., Duchesne, M., Fath, I., Landais, D., Jacquet, M., Tocque, B. Oncogene (1993) [Pubmed]
  11. Two subclasses of guanine exchange factor (GEF) domains revealed by comparison of activities of chimeric genes constructed from CDC25, SDC25 and BUD5 in Saccharomyces cerevisiae. Camus, C., Boy-Marcotte, E., Jacquet, M. Mol. Gen. Genet. (1994) [Pubmed]
  12. SDC25, a dispensable Ras guanine nucleotide exchange factor of Saccharomyces cerevisiae differs from CDC25 by its regulation. Boy-Marcotte, E., Ikonomi, P., Jacquet, M. Mol. Biol. Cell (1996) [Pubmed]
  13. Properties of the catalytic domain of sdc25p, a yeast GDP/GTP exchange factor of Ras proteins. Complexation with wild-type Ras2p, [S24N]Ras2p and [R80D, N81D]Ras2p. Poullet, P., Créchet, J.B., Bernardi, A., Parmeggiani, A. Eur. J. Biochem. (1995) [Pubmed]
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