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Papers In Press, published online ahead of print June 29, 2001
J. Biol. Chem, 10.1074/jbc.M011743200
Submitted on December 27, 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
Binding of ATP
S, a non-hydrolyzable analog of ATP, to RFC (Replication Factor C with a N-terminal truncation (
2-273) of the Rfc1 subunit) was studied by filter binding. RFC alone bound 1.8 ATPS molecules. However, when either PCNA or primer/template DNA were also present 2.6 or 2.7 ATPS molecules, respectively were bound. When both PCNA and DNA were present 3.6 ATPS molecules were bound per RFC. Order of addition experiments using surface plasmon resonance indicate that RFC forms an ATP-mediated binary complex with PCNA prior to formation of a ternary DNA-PCNA-RFC complex. An ATP-mediated complex between RFC and DNA was not competent for binding PCNA and the RFC-DNA complex dissociated with hydrolysis of ATP. Based on these experiments a model is proposed in which: (i) RFC binds two ATPs (RFC-ATP2); (ii) this complex binds PCNA (PCNA-RFC-ATP2), which (iii) goes through a conformational change to reveal a binding site for one additional ATP (PCNA-RFC-ATP3); (iv) this complex can bind DNA to yield DNA-PCNA-RFC-ATP3; (v) a conformational change in the latter complex reveals a fourth binding site for ATP; (vi) the DNA-PCNA-RFC-ATP4 complex is finally competent for completion of PCNA loading and release of RFC upon hydrolysis of ATP.
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