Title : 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.

Pub. Date : 1995 Jan 15

PMID : 7851434






3 Functional Relationships(s)
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1 The highly purified (greater than 95%) stable fusion protein, obtained by affinity chromatography, was very active in enhancing the dissociation rate or the GDP/GTP exchange of the GDP complex of Ras2p or human H-ras p21. Guanosine Triphosphate Ras family GTPase RAS2 Saccharomyces cerevisiae S288C
2 The stimulation of the guanine nucleotide release by Sdc25p-C was stronger for Ras2p.GDP than Ras2p.GTP, an effect that was less pronounced in the case of the p21 complexes. Guanosine Triphosphate Ras family GTPase RAS2 Saccharomyces cerevisiae S288C
3 The association rate of the Ras2p.GDP (GTP) complex was also enhanced by Sdc25p-C. Monovalent and divalent salts inhibit the nucleotide-releasing activity of Sdc25p-C. Guanosine Triphosphate Ras family GTPase RAS2 Saccharomyces cerevisiae S288C