Direct interaction between mammalian DNA polymerase beta and proliferating cell nuclear antigen |
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Authors: | Kedar Padmini S Kim Soon-Jong Robertson Anthony Hou Esther Prasad Rajendra Horton Julie K Wilson Samuel H |
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Affiliation: | Laboratory of Structural Biology, NIEHS/National Institutes of Health, 111 T.W. Alexander Drive, Research Triangle Park, NC 27709, USA. |
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Abstract: | Proliferating cell nuclear antigen (PCNA) plays an essential role in nucleic acid metabolism as a component of the DNA replication and DNA repair machinery. As such, PCNA interacts with many proteins that have a sequence motif termed the PCNA interacting motif (PIM) and also with proteins lacking a PIM. Three regions in human and rat DNA polymerases beta (beta-pol) that resemble the consensus PIM were identified, and we show here that beta-polymerase and PCNA can form a complex both in vitro and in vivo. Immunoprecipitation experiments, yeast two-hybrid analysis, and overlay binding assays were used to examine the interaction between the two proteins. Competition experiments with synthetic PIM-containing peptides suggested the importance of a PIM in the interaction, and studies of a beta-polymerase PIM mutant, H222A/F223A, demonstrated that this alteration blocked the interaction with PCNA. The results indicate that at least one of the PIM-like sequences in beta-polymerase appears to be a functional PIM and was required in the interaction between beta-polymerase and PCNA. |
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