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Replication clamps and clamp loaders.

Authors: Hedglin, M  Kumar, R  Benkovic, SJ 
Citation: Hedglin M, etal., Cold Spring Harb Perspect Biol. 2013 Apr 1;5(4):a010165. doi: 10.1101/cshperspect.a010165.
Pubmed: (View Article at PubMed) PMID:23545418
DOI: Full-text: DOI:10.1101/cshperspect.a010165

To achieve the high degree of processivity required for DNA replication, DNA polymerases associate with ring-shaped sliding clamps that encircle the template DNA and slide freely along it. The closed circular structure of sliding clamps necessitates an enzyme-catalyzed mechanism, which not only opens them for assembly and closes them around DNA, but specifically targets them to sites where DNA synthesis is initiated and orients them correctly for replication. Such a feat is performed by multisubunit complexes known as clamp loaders, which use ATP to open sliding clamp rings and place them around the 3' end of primer-template (PT) junctions. Here we discuss the structure and composition of sliding clamps and clamp loaders from the three domains of life as well as T4 bacteriophage, and provide our current understanding of the clamp-loading process.


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RGD Object Information
RGD ID: 7246932
Created: 2013-06-24
Species: All species
Last Modified: 2013-06-24
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.