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Originally published In Press as doi:10.1074/jbc.M206202200 on August 20, 2002

J. Biol. Chem., Vol. 277, Issue 43, 40871-40880, October 25, 2002
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Mouse Geminin Inhibits Not Only Cdt1-MCM6 Interactions but Also a Novel Intrinsic Cdt1 DNA Binding Activity*

Ken-ichiro YanagiDagger §, Takeshi MizunoDagger ||, Zhiying YouDagger **, and Fumio HanaokaDagger §||Dagger Dagger

From the Dagger  Cellular Physiology Laboratory, RIKEN (The Institute of Physical and Chemical Research) and || CREST, Japan Science and Technology Corporation, Wako, Saitama 351-0198, Japan and the § Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan

DNA replication is controlled by the stepwise assembly of a pre-replicative complex and the replication apparatus. Cdt1 is a novel component of the pre-replicative complex and plays a role in loading the minichromosome maintenance (MCM) 2-7 complex onto chromatin. Cdt1 activity is inhibited by geminin, which is essential for the G2/M transition in metazoan cells. To understand the molecular basis of the Cdt1-geminin regulatory mechanism in mammalian cells, we cloned and expressed the mouse Cdt1 homologue cDNA in bacterial cells and purified mouse Cdt1 to near homogeneity. We found by yeast two-hybrid analysis that mouse Cdt1 associates with geminin, MCM6, and origin recognition complex 2. MCM6 interacts with the Cdt1 carboxyl-terminal region (amino acids 407-477), which is conserved among eukaryotes, whereas geminin associates with the Cdt1 central region (amino acids 177-380), which is conserved only in metazoans. In addition, we found that Cdt1 can bind DNA in a sequence-, strand-, and conformation-independent manner. The Cdt1 DNA binding domain overlaps with the geminin binding domain, and the binding of Cdt1 to DNA is inhibited by geminin. Taken together, we have defined structural domains and novel biochemical properties for mouse Cdt1 that suggest that Cdt1 behaves as an intrinsic DNA binding factor in the pre-replicative complex.

* This work was supported by grants from the Ministry of Education, Culture, Sports, Science, and Technology of Japan, a special grant for the promotion of research from RIKEN, and a grant from the Bioarchitect Research Project of RIKEN.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.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AB086655.

Contributed equally to this work.

** Special postdoctoral researcher of RIKEN. Present address: Dept. of Cell Biology, Tokyo Metropolitan Inst. of Medical Science, Bunkyo-ku, Tokyo 113-8613, Japan.

Dagger Dagger To whom correspondence should be addressed: Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565-0871, Japan. Tel.: 81-6-6879-7975; Fax: 81-6-6877-9382; E-mail address: fhanaoka@fbs.osaka-u.ac.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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