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J. Biol. Chem., Vol. 276, Issue 37, 34776-34783, September 14, 2001
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From the Department of Biochemistry and Molecular Biophysics,
Washington University School of Medicine,
St. Louis, Missouri 63110
Binding of adenosine (3-thiotriphosphate)
(ATP
S), a nonhydrolyzable analog of ATP, to replication factor C
with a N-terminal truncation (
2-273) of the Rfc1 subunit (RFC) 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 goes through a conformational
change to reveal a binding site for one additional ATP
(PCNA·RFC·ATP3); (iii) this complex can bind DNA to
yield DNA·PCNA·RFC·ATP3; (iv) a conformational change
in the latter complex reveals a fourth binding site for ATP; and (v)
the DNA·PCNA·RFC·ATP4 complex is finally competent
for completion of PCNA loading and release of RFC upon hydrolysis of ATP.
To whom correspondence should be addressed: Dept. of
Biochemistry and Molecular Biophysics, Washington University
School of Medicine, 660 S. Euclid Ave., St. Louis, MO 63110. E-mail: burgers@biochem.wustl.edu.
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