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(Received for publication, January 31, 1997, and in revised form, February 24, 1997)
From the Departments of Molecular Biology and Cell Biology, The
Scripps Research Institute, La Jolla, California 92037
The Schizosaccharomyces pombe gene
pch1+ (pombe cyclin
C homology) was isolated in a two-hybrid screen
for proteins that interact with Cdc2. The cyclin box region of Pch1
protein shares greatest sequence identity with mammalian and
Drosophila C-type cyclins (~33% identity). Pch1 is
significantly less similar to Mcs2 (19% identity), a second member of
the C-type cyclin family in S. pombe. Cdc2 co-precipitates
with Pch1 in S. pombe cell lysates, although Cdc2 may not
be the major catalytic partner of a Pch1 kinase in vivo.
Purified Pch1-associated kinase phosphorylated myelin basic protein,
histone H1, and a peptide corresponding to the carboxyl-terminal domain
repeat of RNA polymerase II. The amount of pch1 mRNA
does not oscillate during the cell cycle, as is the case for mRNA
transcripts of other C-type cyclin genes.
Volume 272, Number 18,
Issue of May 2, 1997
pp. 12100-12106
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
pch1 cells are
inviable, therefore S. pombe has two essential genes that
encode members of the C-type cyclin family,
pch1+ and mcs2+. The
pch1 mutation causes pleiotropic morphological defects and an associated growth deficiency, but loss of Pch1 activity does not
result in a cdc cell cycle-arrest phenotype.
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