Cyclin B Proteolysis and the Cyclin-dependent Kinase Inhibitor rum1p Are Required for Pheromone-induced G1 Arrest in Fission Yeast

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Vol. 9, Issue 6, 1309-1321, June 1998

Cyclin B Proteolysis and the Cyclin-dependent Kinase Inhibitor rum1p Are Required for Pheromone-induced G₁ Arrest in Fission Yeast

Bodo Stern,^* and Paul Nurse

Department of Physiology, University of California, San Francisco, San Francisco, California, 94143-0444

The blocking of G₁ progression by fission yeast pheromones requires inhibition of the cyclin-dependent kinase cdc2p associatedwith the B-cyclins cdc13p and cig2p. We show that cyclosome-mediateddegradation of cdc13p and cig2p is necessary for down-regulationof B-cyclin-associated cdc2p kinase activity and for phermone-inducedG₁ arrest. The cyclin-dependent kinase inhibitor rum1p is alsorequired to maintain this G₁ arrest; it binds both cdc13p andcig2p and is specifically required for cdc13p proteolysis. Wepropose that rum1p acts as an adaptor targeting cdc13p for degradationby the cyclosome. In contrast, the cig2p-cdc2p kinase can be down-regulated,and the cyclin cig2p can be proteolyzed independently of rum1p.We suggest that pheromone signaling inhibits the cig2p-cdc2p kinase,bringing about a transient G₁ arrest. As a consequence, rum1plevels increase, thus inhibiting and inducing proteolysis of thecdc13p-cdc2p kinase; this is necessary to maintain G₁ arrest.We have also shown that pheromone-induced transcription occursonly in G₁ and is independent of rum1p.

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