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Papers In Press, published online ahead of print July 4, 2003
J. Biol. Chem, 10.1074/jbc.M306049200
Submitted on June 9, 2003
Revised on July 1, 2003
Accepted on July 4, 2003
Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, WI 53226
Corresponding Author: mlei{at}mcw.edu
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 (~ 800kD). 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. 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.
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