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Vol. 9, Issue 6, 1309-1321, June 1998
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
associated with the B-cyclins cdc13p and cig2p. We show that
cyclosome-mediated degradation of cdc13p and cig2p is necessary for
down-regulation of B-cyclin-associated cdc2p kinase activity and for
phermone-induced G1 arrest. The cyclin-dependent kinase
inhibitor rum1p is also required to maintain this G1
arrest; it binds both cdc13p and cig2p and is specifically required for
cdc13p proteolysis. We propose that rum1p acts as an adaptor targeting
cdc13p for degradation by 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, rum1p levels increase, thus inhibiting and
inducing proteolysis of the cdc13p-cdc2p kinase; this is necessary to
maintain G1 arrest. We have also shown that
pheromone-induced transcription occurs only in G1 and is
independent of rum1p.
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