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J. Biol. Chem., Vol. 275, Issue 21, 16235-16241, May 26, 2000
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From the A strong body of evidence indicates that
cyclin-dependent protein kinases are required not only for
the initiation of DNA replication but also for preventing
over-replication in eukaryotic cells. Mcm proteins are one of the
components of the replication licensing system that permits only a
single round of DNA replication per cell cycle. It has been reported
that Mcm proteins are phosphorylated by the
cyclin-dependent kinases in vivo, suggesting
that these two factors are cooperatively involved in the regulation of
DNA replication. Our group has reported that a 600-kDa Mcm4,6,7 complex has a DNA helicase activity that is probably necessary for the initiation of DNA replication. Here, we examined the in
vitro phosphorylation of the Mcm complexes with cyclin A/Cdk2 to
understand the interplay between Mcm proteins and
cyclin-dependent kinases. The cyclin A/Cdk2 mainly
phosphorylated the amino-terminal region of Mcm4 in the Mcm4,6,7
complex. The phosphorylation was associated with the inactivation of
its DNA helicase activity. These results raise the possibility that the
inactivation of Mcm4,6,7 helicase activity by Cdk2 is a part of the
system for regulating DNA replication.
Inhibition of Mcm4,6,7 Helicase Activity by Phosphorylation
with Cyclin A/Cdk2*
§,,,, and Mitsubishi Kasei Institute of Life Sciences,
11 Minamiooya, Machida, Tokyo 194-8511 and the ¶ Department of
Molecular and Cellular Biology, Medical Institute of Bioregulation,
Kyushu University, 3-1-1 Maidashi,
Higashi-ku, Fukuoka 812-8582, Japan
*
This work was supported in part by a grant-in-aid for
Scientific Research on Priority Area from the Ministry of Education, Science, and Culture of Japan.The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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