Interaction of the β Sliding Clamp with MutS, Ligase, and DNA Polymerase I

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 98; no. 15; pp. 8376 - 8380
• Main Authors: Francisco J. López de Saro, Mike O'Donnell
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 17.07.2001; National Acad Sciences; The National Academy of Sciences
• Series: Colloquium Paper
• Subjects: Adenosine Triphosphatases; Bacterial Proteins - metabolism; Base Pair Mismatch; Cell growth; Cell nucleus; Colloquium: Links between Recombination and Replication: Vital Roles of Recombination; Deoxyribonucleic acid; DNA; DNA Ligases - metabolism; DNA mismatch repair; 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; Escherichia coli Proteins; Gels; Genetics; Humans; Mathematical rings; MutS DNA Mismatch-Binding Protein; MutS protein; Phosphorylation; Polymers; Proliferating Cell Nuclear Antigen - metabolism; Proteins; RNA; Trans-Activators - metabolism; Viral Proteins - metabolism
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.121009498

The β 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 β clamp is known to function with DNA polymerases II and V, indicating that β also interacts with more than just the chromosomal replicase, DNA polymerase III. This report demonstrates three previously undetected protein-protein interactions with the β clamp. Thus, β 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 β interactive proteins suggests that the prokaryotic β ring participates in a wide variety of reactions beyond its role in chromosomal replication.