期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2001
卷号：98
期号：15
页码：8376-8380
DOI：10.1073/pnas.121009498
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
