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Science 26 August 1994:
Vol. 265. no. 5176, pp. 1228 - 1231
DOI: 10.1126/science.8066461
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Articles

Science, Vol 265, Issue 5176, 1228-1231
Copyright © 1994 by American Association for the Advancement of Science

articles

Direct inhibition of the yeast cyclin-dependent kinase Cdc28-Cln by Far1

M Peter and I Herskowitz

Department of Biochemistry and Biophysics, University of California at San Francisco 94143-0448.

Cell cycle arrest of Saccharomyces cerevisiae in G1 by the antimitogen alpha-factor is mediated by activation of a signal transduction pathway that results in inhibition of the cyclin-dependent kinase Cdc28-Cln. The Far1 protein is required for cell cycle arrest and associates with the Cdc28-Cln complex. The kinase activity of Cdc28-Cln was directly inhibited by Far1 both in vivo and in vitro, thus demonstrating that Far1 acts at the final step in the alpha-factor response pathway by inhibiting a G1 cyclin-dependent kinase.


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