Bochman ML and Schwacha A (2008) The Mcm2-7 complex has in vitro helicase activity. Mol Cell 31(2):287-93
Abstract: Helicases unwind duplex DNA ahead of the polymerases at the replication fork. However, the identity of the eukaryotic replicative helicase has been controversial; in vivo studies implicate the ring-shaped heterohexameric Mcm2-7 complex, although only a specific subset of Mcm subunits (Mcm467) unwind DNA in vitro. To address this discrepancy, we have compared both Mcm assemblies and find that they differ in their linear single-stranded DNA association rate and their ability to bind circular single-stranded DNA. These differences depend upon the Mcm2/5 interface, which we hypothesize serves as an ATP-dependent "gate" within Mcm2-7. Importantly, we find that reaction conditions that putatively close the Mcm2-7 "gate" reconstitute Mcm2-7 helicase activity. Unlike Mcm467, Mcm2-7 helicase activity is strongly anion dependent. Our results show that purified Mcm2-7 acts as a helicase, provides functional evidence of a Mcm2/5 gate, and lays the foundation for future mechanistic studies of this critical factor.
|Status: Published||Type: Journal Article | Research Support, Non-U.S. Gov't||PubMed ID: 18657510|
Topics addressed in this paper
Number of different genes curated to this paper: 6
- To find other papers on a gene and topic, click on the colored ball in the appropriate box.
- displays other papers with information about that topic for that gene.
- displays other papers in SGD that are associated with that topic.
The topic is addressed in these papers but does not describe a specific gene or chromosomal feature.
- To go to the Locus page for a gene, click on the gene name.