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  • Title: In vitro interaction between Saccharomyces cerevisiae CDC25 and RAS2 proteins.
    Author: Baroni MD, Marconi G, Parrini MC, Monti P, Alberghina L.
    Journal: Biochem Biophys Res Commun; 1992 Jul 15; 186(1):467-74. PubMed ID: 1632785.
    Abstract:
    In Saccharomyces cerevisiae the CDC25 protein is a positive regulator of RAS/cAMP pathway [1-4], enhancing the GDP-releasing rate of RAS2 protein [5]. In this work we have tried to detect a direct interaction between CDC25 and RAS2 gene products. The results indicate that both the whole RAS2 protein and a truncated version that lacks approximately 25 C-terminal residues interact specifically with the CDC25 protein. On the contrary, a derivative of RAS2 that lacks the 112 C-terminal residues as well as the p21TI-ras is not able to bind the CDC25 protein in our assay conditions. The 310 C-terminal aminoacids of CDC25 bind RAS2 while a C-terminus deletion within this aminoacid stretch abolishes the binding. The possible physiological significance of these findings is discussed.
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