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Papers In Press, published online ahead of print June 29, 2001
J. Biol. Chem, 10.1074/jbc.M011633200
Submitted on December 22, 2000
Revised on May 3, 2001
Accepted on June 28, 2001
Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110
Corresponding Author: burgers{at}biochem.wustl.edu
The conserved lysine in the Walker A motif of the ATP-binding domain encoded by the yeast RFC1, RFC2, RFC3 and RFC4 genes was mutated to glutamic acid. RFC complexes (Replication Factor C with a N-terminal truncation (
2-273) of the Rfc1 subunit) containing a single mutant subunit were overproduced in E. coli for biochemical analysis. All of the mutant RFC complexes were capable of interacting with PCNA. Complexes containing a rfc1-K359E mutation were similar to wild type in replication activity and ATPase activity, however, the mutant complex showed increased susceptibility to proteolysis. In contrast, complexes containing either a rfc2-K71E mutation or a rfc3-K59E mutation were severely impaired in ATPase and clamp loading activity. In addition to their defects in ATP hydrolysis these complexes were defective for DNA-binding. A mutant complex containing the rfc4-K55E mutation performed as well as a wild type complex in clamp loading, but only at very high ATP concentrations. Mutant RFC complexes containing rfc2-K71R or rfc3-K59R, carrying a conservative lysine->arginine mutation, had much milder clamp loading defects which could be partially (rfc2-K71R) or completely (rfc3-K59R) suppressed at high ATP concentrations.
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