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Microbiology and Molecular Biology Reviews, December 2009, p. 652-683, Vol. 73, No. 4
1092-2172/09/$08.00+0     doi:10.1128/MMBR.00019-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The Mcm Complex: Unwinding the Mechanism of a Replicative Helicase

Matthew L. Bochman1,2 and Anthony Schwacha2*

Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544,1 Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 152602

Summary: The Mcm2-7 complex serves as the eukaryotic replicative helicase, the molecular motor that both unwinds duplex DNA and powers fork progression during DNA replication. Consistent with its central role in this process, much prior work has illustrated that Mcm2-7 loading and activation are landmark events in the regulation of DNA replication. Unlike any other hexameric helicase, Mcm2-7 is composed of six unique and essential subunits. Although the unusual oligomeric nature of this complex has long hampered biochemical investigations, recent advances with both the eukaryotic as well as the simpler archaeal Mcm complexes provide mechanistic insight into their function. In contrast to better-studied homohexameric helicases, evidence suggests that the six Mcm2-7 complex ATPase active sites are functionally distinct and are likely specialized to accommodate the regulatory constraints of the eukaryotic process.

* Corresponding author. Mailing address: Department of Biological Sciences, University of Pittsburgh, 4249 Fifth Avenue, 560 Crawford Hall, Pittsburgh, PA 15260. Phone: (412) 624-4307. Fax: (412) 624-4759. E-mail: Schwacha{at}pitt.edu

Microbiology and Molecular Biology Reviews, December 2009, p. 652-683, Vol. 73, No. 4
1092-2172/09/$08.00+0     doi:10.1128/MMBR.00019-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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