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Related Experiment Videos

Clamp loaders and sliding clamps.

David Jeruzalmi1, Mike O'Donnell, John Kuriyan

  • 1Department of Molecular and Cell Biology, Howard Hughes Medical Institute, The University of California, Berkeley, CA 94720, USA.

Current Opinion in Structural Biology
|April 18, 2002
PubMed
Summary

Structural studies reveal the ring-shaped DNA polymerase sliding clamps and clamp loaders. These findings clarify how these processivity factors interact with DNA polymerase and how ATP binding facilitates clamp loading.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • DNA polymerase processivity factors, including sliding clamps and clamp loaders, are crucial for efficient DNA replication.
  • Understanding their structure and function is key to comprehending DNA replication fidelity and speed.

Purpose of the Study:

  • To provide a coherent view of the structure and function of DNA polymerase processivity factors.
  • To elucidate the structural basis of clamp-DNA polymerase interactions.
  • To model the mechanism of ATP-dependent clamp loading.

Main Methods:

  • X-ray crystallography was used to determine the structures of sliding clamps from bacteriophages T4 and RB69, and an archaeal species.
  • Crystallography and electron microscopy provided insights into the architecture of clamp loaders from diverse organisms.

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  • Structural data was integrated to develop models of clamp-DNA polymerase interaction and clamp loader function.

    • Main Results:

    • Crystal structures revealed diverse ring-shaped sliding clamps and clarified their interaction with DNA polymerase.
    • Structural and electron microscopic analyses highlighted a conserved architecture among bacterial, archaeal, and eukaryotic clamp loaders.
    • Models were generated illustrating the coupling of ATP binding to clamp opening and loading.

    Conclusions:

    • Recent structural studies offer a unified understanding of DNA polymerase sliding clamps and clamp loaders.
    • The findings clarify the molecular mechanisms underlying DNA replication processivity.
    • This work provides a foundation for further investigations into DNA replication machinery.