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Papers In Press, published online ahead of print February 10, 2003
Laboratory of DNA Replication, Rockefeller University, New York, NY 10021
Corresponding Author: johnsoa{at}mail.rockefeller.edu
The
J. Biol. Chem, 10.1074/jbc.M212708200
Submitted on December 13, 2002
Revised on February 6, 2003
Accepted on February 10, 2003
Ordered hydrolysis in the
complex clamp loader AAA+ machine
complex couples ATP hydrolysis to the loading of 
sliding clamps onto DNA for processive replication. The complex structure shows that the clamp loader subunits are arranged as a circular heteropentamer. The three motor subunits bind ATP, the 
wrench opens the ring, and the ’ stator modulates the - interaction. Neither nor ’ bind ATP. This report demonstrates that the ’ stator contributes a catalytic arginine for hydrolysis of ATP bound to the adjacent 1 subunit. Thus, the ’ stator contributes to the motor function of the trimer. Mutation of arginine 169 of , which removes the catalytic arginines from only the 2 and 3 ATP sites, abolishes ATPase activity even though ATP Site 1 is intact and all three sites are filled. This result implies that hydrolysis of the three ATP molecules occurs in a particular order, the reverse of ATP binding, where ATP in Site 1 is not hydrolyzed until ATP in Sites 2 and/or 3 is hydrolyzed. Implications of these results to clamp loaders of other systems are discussed.
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