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Vol. 12, Issue 5, 1257-1274, May 2001
and
*Departments of Molecular and Developmental Biology and
§Molecular Biology, Institute of Medical Science,
University of Tokyo, Tokyo 108-8639, Japan; ¶The Kitasato
Institute, Tokyo 108-0072, Japan; and Hsk1, Saccharomyces cerevisiae Cdc7-related kinase
in Shizosaccharomyces pombe, is required for G1/S
transition and its kinase activity is controlled by the regulatory
subunit Dfp1/Him1. Analyses of a newly isolated temperature-sensitive
mutant, hsk1-89, reveal that Hsk1 plays crucial roles in
DNA replication checkpoint signaling and maintenance of proper
chromatin structures during mitotic S phase through regulating the
functions of Rad3 (ATM)-Cds1 and Rad21 (cohesin), respectively, in
addition to expected essential roles for initiation of mitotic DNA
replication through phosphorylating Cdc19 (Mcm2). Checkpoint defect in
hsk1-89 is indicated by accumulation of
cut cells at 30°C. hsk1-89 displays
synthetic lethality in combination with rad3 deletion,
indicating that survival of hsk1-89 depends on
Rad3-dependent checkpoint pathway. Cds1 kinase activation, which
normally occurs in response to early S phase arrest by nucleotide deprivation, is largely impaired in hsk1-89.
Furthermore, Cds1-dependent hyperphosphorylation of Dfp1 in response to
hydroxyurea arrest is eliminated in hsk1-89,
suggesting that sufficient activation of Hsk1-Dfp1 kinase is required
for S phase entry and replication checkpoint signaling.
hsk1-89 displays apparent defect in mitosis at 37°C
leading to accumulation of cells with near 2C DNA content and with
aberrant nuclear structures. These phenotypes are similar to those of
rad21-K1 and are significantly enhanced in a
hsk1-89 rad21-K1 double mutant. Consistent with
essential roles of Rad21 as a component for the cohesin complex, sister
chromatid cohesion is partially impaired in hsk1-89,
suggesting a possibility that infrequent origin firing of the mutant
may affect the cohesin functions during S phase.
Core Research for
Engineering, Science, and Technology, Japan Science and Technology
Corporation, Tokyo 108-8639, Japan; Department of Cell
Biology, Tokyo Metropolitan Institute of Medical Science, Tokyo
113-8613
Corresponding author.
E-mail address: ttakeda{at}ims.u-tokyo.ac.jp.
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