In vitro interaction between Saccharomyces cerevisiae CDC25 and RAS2 proteins

Maurizio D. Baroni, Giulia Marconi, M. Carla Parrini, Paolo Monti, Lilia Alberghina

Research output: Contribution to journalArticle

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 p21H-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.

Original languageEnglish
Pages (from-to)467-474
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume186
Issue number1
DOIs
Publication statusPublished - Jul 15 1992

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Fingerprint Dive into the research topics of 'In vitro interaction between Saccharomyces cerevisiae CDC25 and RAS2 proteins'. Together they form a unique fingerprint.

  • Cite this