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Nucleic Acids Research 2005 33(15):4940-4950; doi:10.1093/nar/gki807
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Published online 8 September 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Interactions between the archaeal Cdc6 and MCM proteins modulate their biochemical properties

Rajesh Kasiviswanathan, Jae-Ho Shin and Zvi Kelman*

University of Maryland Biotechnology Institute, Center for Advanced Research in Biotechnology 9600 Gudelsky Drive, Rockville, MD 20850, USA

*To whom correspondence should be addressed. Tel: +1 240 314 6294; Fax: +1 240 314 6255; Email: kelman{at}umbi.umd.edu

Received June 8, 2005. Revised August 15, 2005. Accepted August 15, 2005.

The origin recognition complex, Cdc6 and the minichromosome maintenance (MCM) complex play essential roles in the initiation of eukaryotic DNA replication. Homologs of these proteins may play similar roles in archaeal replication initiation. While the interactions among the eukaryotic initiation proteins are well documented, the protein–protein interactions between the archaeal proteins have not yet been determined. Here, an extensive structural and functional analysis of the interactions between the Methanothermobacter thermautotrophicus MCM and the two Cdc6 proteins (Cdc6-1 and -2) identified in the organism is described. The main contact between Cdc6 and MCM occurs via the N-terminal portion of the MCM protein. It was found that Cdc6–MCM interaction, but not Cdc6–DNA binding, plays the predominant role in regulating MCM helicase activity. In addition, the data showed that the interactions with MCM modulate the autophosphorylation of Cdc6-1 and -2. The results also suggest that MCM and DNA may compete for Cdc6-1 protein binding. The implications of these observations for the initiation of archaeal DNA replication are discussed.


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