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Papers In Press, published online ahead of print June 29, 2001
Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110
Corresponding Author: burgers{at}biochem.wustl.edu
Eukaryotic Replication Factor C (RFC) is the heteropentameric complex that loads the replication clamp PCNA onto primed DNA. In this study we used a derivative of RFC with a N-terminal truncation of the Rfc1 subunit removing a DNA-binding domain not required for clamp loading. Interactions of yeast RFC with PCNA and DNA were studied by surface plasmon resonance. Binding of RFC to PCNA was stimulated by either ATP
J. Biol. Chem, 10.1074/jbc.M011631200
Submitted on December 22, 2000
Revised on May 3, 2001
Accepted on June 28, 2001
ATP utilization by yeast replication factor C.I.ATP-mediated interaction with DNA and with PCNA
S or ATP. RFC bound only to primer/template DNA coated with the single-stranded DNA binding protein RPA if ATPS was also present. Binding occurred without dissociation of RPA. ATP did not stimulate binding of RFC to DNA suggesting that hydrolysis of ATP dissociated DNA-bound RFC. However, when RFC and PCNA together were flowed across the DNA-chip in the presence of ATP, a signal was observed suggesting loading of PCNA by RFC. With ATPS present instead of ATP, long-lived response signals were observed indicative of loading complexes arrested on the DNA. A primer with a 3’-single stranded extension also allowed loading of PCNA, yet turnover of the reaction intermediates was dramatically slowed down. Filter binding experiments and analysis of proteins bound to DNA-magnetic beads confirmed the conclusions drawn from the surface plasmon resonance studies.
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