PMID:11459978
Citation |
López de Saro, FJ and O'Donnell, M (2001) Interaction of the beta sliding clamp with MutS, ligase, and DNA polymerase I. Proc. Natl. Acad. Sci. U.S.A. 98:8376-80 |
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Abstract |
The beta and proliferating cell nuclear antigen (PCNA) sliding clamps were first identified as components of their respective replicases, and thus were assigned a role in chromosome replication. Further studies have shown that the eukaryotic clamp, PCNA, interacts with several other proteins that are involved in excision repair, mismatch repair, cellular regulation, and DNA processing, indicating a much wider role than replication alone. Indeed, the Escherichia coli beta clamp is known to function with DNA polymerases II and V, indicating that beta also interacts with more than just the chromosomal replicase, DNA polymerase III. This report demonstrates three previously undetected protein-protein interactions with the beta clamp. Thus, beta interacts with MutS, DNA ligase, and DNA polymerase I. Given the diverse use of these proteins in repair and other DNA transactions, this expanded list of beta interactive proteins suggests that the prokaryotic beta ring participates in a wide variety of reactions beyond its role in chromosomal replication. |
Links |
PubMed PMC37446 Online version:10.1073/pnas.121009498 |
Keywords |
Adenosine Triphosphatases; Bacterial Proteins/metabolism; Base Pair Mismatch; DNA Ligases/metabolism; DNA Polymerase I/metabolism; DNA Polymerase II/metabolism; DNA Polymerase III/metabolism; DNA Repair; DNA Replication; DNA-Binding Proteins; DNA-Directed DNA Polymerase/metabolism; Escherichia coli Proteins; Humans; MutS DNA Mismatch-Binding Protein; Proliferating Cell Nuclear Antigen/metabolism; Trans-Activators/metabolism; Viral Proteins/metabolism |
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