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Clamp loader ATPases and the evolution of DNA replication machinery

Brian A Kelch13*, Debora L Makino137, Mike O'Donnell6 and John Kuriyan12345

Author affiliations

1 Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA

2 Department of Chemistry, University of California, Berkeley, CA 94720, USA

3 California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720, USA

4 Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA

5 Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA

6 Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021, USA

7 Max-Planck Institute of Biochemistry, Department of Structural Cell Biology, D-82152 Martinsried, Germany

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Citation and License

BMC Biology 2012, 10:34  doi:10.1186/1741-7007-10-34

Published: 20 April 2012

Abstract

Clamp loaders are pentameric ATPases of the AAA+ family that operate to ensure processive DNA replication. They do so by loading onto DNA the ring-shaped sliding clamps that tether the polymerase to the DNA. Structural and biochemical analysis of clamp loaders has shown how, despite differences in composition across different branches of life, all clamp loaders undergo the same concerted conformational transformations, which generate a binding surface for the open clamp and an internal spiral chamber into which the DNA at the replication fork can slide, triggering ATP hydrolysis, release of the clamp loader, and closure of the clamp round the DNA. We review here the current understanding of the clamp loader mechanism and discuss the implications of the differences between clamp loaders from the different branches of life.