Journal
EMBO JOURNAL
Volume 22, Issue 23, Pages 6408-6418Publisher
WILEY
DOI: 10.1093/emboj/cdg603
Keywords
beta-clamp; clamp loader; DNA polymerase; DNA repair; PCNA; RFC
Categories
Funding
- NIGMS NIH HHS [R01 GM021422, R37 GM038839, R37 GM021422, R01 GM038839, GM38839, GM21422, GM42554] Funding Source: Medline
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Protein clamps are ubiquitous and essential components of DNA metabolic machineries, where they serve as mobile platforms that interact with a large variety of proteins. In this report we identify residues that are required for binding of the beta-clamp to DNA polymerase III of Escherichia coli, a polymerase of the Pol C family. We show that the alpha polymerase subunit of DNA polymerase III interacts with the beta-clamp via its extreme seven C-terminal residues, some of which are conserved. Moreover, interaction of Pol III with the clamp takes place at the same site as that of the delta-subunit of the clamp loader, providing the basis for a switch between the clamp loading machinery and the polymerase itself. Escherichia coli DNA polymerases I, II, IV and V (UmuC) interact with beta at the same site. Given the limited amounts of clamps in the cell, these results suggest that clamp binding may be competitive and regulated, and that the different polymerases may use the same clamp sequentially during replication and repair.
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