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Science 18 May 1990:
Vol. 248. no. 4957, pp. 866 - 868
DOI: 10.1126/science.2188363
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Articles

Science, Vol 248, Issue 4957, 866-868
Copyright © 1990 by American Association for the Advancement of Science

articles

Enhancement of the GDP-GTP exchange of RAS proteins by the carboxyl-terminal domain of SCD25

JB Crechet, P Poullet, MY Mistou, A Parmeggiani, J Camonis, E Boy-Marcotte, F Damak, and M Jacquet

Laboratoire de Biochimie, URA 240 du CNRS, Ecole Polytechnique, Palaiseau, France.

In Saccharomyces cerevisiae, the product of the CDC25 gene controls the RAS-mediated production of adenosine 3',5'-monophosphate (cAMP). In vivo the carboxyl-terminal third of the CDC25 gene product is sufficient for the activation of adenylate cyclase. The 3'-terminal part of SCD25, a gene of S. cerevisiae structurally related to CDC25, can suppress the requirement for CDC25. 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. This protein fragment had a similar effect on the human c-H-ras-encoded p21 protein. Thus, the SCD25 carboxyl-terminal domain can enhance the regeneration of the active form of RAS proteins.


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