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J. Biol. Chem., Vol. 278, Issue 38, 36051-36058, September 19, 2003

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A Novel Zinc Finger Is Required for Mcm10 Homocomplex Assembly^*

Craig R. Cook  , Guosheng Kung , Francis C. Peterson ¶, Brian F. Volkman ¶ and Ming Lei  ||

From the Departments of Microbiology and Molecular Genetics and ^¶Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226

Mcm10 is a DNA replication factor that interacts with multiple subunits of the MCM2-7 hexameric complex. We report here that Mcm10 self-interacts and assembles into large homocomplexes (800 kDa). A conserved domain of 210 amino acid residues is sufficient for mediating self-interaction and complex assembly. A novel zinc finger within the conserved domain, CX₁₀CX₁₁CX₂H, is essential for the homocomplex formation. Mutant alleles with amino acid substitutions at conserved cysteines and histidine in the zinc finger fail to assemble homocomplexes. A defect in homocomplex assembly correlates with defects in DNA replication and cell growth in the mutants. These observations suggest that homocomplex assembly is essential for Mcm10 function. Multisubunit Mcm10 homocomplexes may provide the structural basis for Mcm10 to interact with multiple subunits of the MCM2-7 hexamer.

Received for publication, June 9, 2003 , and in revised form, July 1, 2003.

^* This work was supported by National Institutes of Health Grant GM6264901 and American Cancer Society Grant IRG-8600414 (to M. L.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by a Northwestern Mutual postdoctoral fellowship.

^|| To whom correspondence should be addressed. Tel.: 414-456-8321; Fax: 414-456-6535; E-mail: mlei{at}mcw.edu.

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