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Papers In Press, published online ahead of print September 20, 2007
J. Biol. Chem, 10.1074/jbc.M706300200
Submitted on July 31, 2007
Revised on September 10, 2007
Accepted on September 19, 2007

MCM fork substrate specificity involves dynamic interaction with the 5' tail

Eli Rothenberg, Michael A. Trakselis, Stephen D. Bell, and Taekjip Ha

Physics, University of Illinois, Urbana, IL 61801

Corresponding Author: tjha{at}uiuc.edu

The archaeal Minichromosome-Maintenance (MCM) protein forms a homohexameric complex that functions as the DNA replication helicase, and serves as a model system for its eukaryotic counterpart. Here we applied single-molecule fluorescence resonance energy transfer (smFRET) methods to probe the substrate specificity and binding mechanism of the MCM from the hyperthermophilic archaeon Sulfolobus solfataricus (Sso) on various DNA substrates. Sso MCM displays a binding preference for forked substrates relative to partial or full duplex substrates. Moreover, the nature of MCM binding to Yshaped substrates is distinct in that MCM loads on the 3’ tail while interacting with the 5’ tail likely via MCM surface. These results provide the first elucidation of a dynamic nature of interaction between a ring-shaped helicase interacting and an opposing single stranded DNA tail. This interaction contributes to substrate selectivity and increases the stability of the forked DNA-MCM complex, with possible implications for MCM’s unwinding mechanism.


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