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

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TitleInteractions between the archaeal Cdc6 and MCM proteins modulate their biochemical properties.
Publication TypeJournal Article
Year of Publication2005
AuthorsKasiviswanathan, R, Shin, J-H, Kelman, Z
JournalNucleic Acids Res
Volume33
Issue15
Pagination4940-50
Date Published2005
ISSN1362-4962
KeywordsArchaea, Archaeal Proteins, DNA Helicases, DNA Replication, DNA-Binding Proteins, Methanobacteriaceae, Origin Recognition Complex, Phosphorylation, Protein Structure, Tertiary, Two-Hybrid System Techniques
Abstract

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.

DOI10.1093/nar/gki807
Alternate JournalNucleic Acids Res.
PubMed ID16150924
PubMed Central IDPMC1201339