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Papers In Press, published online ahead of print November 10, 2003
Biochemistry & Molecular Biology, University of Florida, Gainesville, FL 32610-0245
Corresponding Author: lbloom{at}ufl.edu
Sliding clamps tether DNA polymerases to DNA to increase the processivity of synthesis. The Escherichia coli
J. Biol. Chem, 10.1074/jbc.M310430200
Submitted on September 22, 2003
Revised on November 3, 2003
Accepted on November 10, 2003
Mechanism of loading the Escherichia coli DNA polymerase III sliding clamp. II.Uncoupling the
and DNA binding activities of the 
complex
complex loads the 
sliding clamp onto DNA in an ATP-dependent reaction in which ATP binding and hydrolysis modulate the affinity of complex for and DNA. This is the second of two reports that addresses the question of how ATP binding and hydrolysis regulate specific interactions with DNA and . Mutations were made to an Arg residue in a conserved SRC motif in the 
’ and subunits that interacts with the ATP site of the neighboring subunit. Mutation of the ’ subunit reduces the ATP-dependent binding activity whereas mutation of the subunits reduces the DNA binding activity of complex. The complex containing the ’ mutation gave a pre-steady-state burst of ATP hydrolysis, but at a reduced rate and amplitude relative to wild-type complex. A pre-steady-state burst of ATP hydrolysis was not observed for the complex containing the mutations consistent with the reduced DNA binding activity of this complex. The differential effects of these mutations suggest that ATP binding at the 1 site may be coupled to conformational changes that largely modulate interactions with whereas ATP binding at 2 and/or 3 may be coupled to conformational changes that have a major role in interactions with DNA. Additionally, these results show that the “arginine fingers” play a structural role in facilitating the formation of a conformation that has high affinity for and DNA.
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