Phosphorylation of the p68 Subunit of Pol δ Acts as a Molecular Switch To Regulate Its Interaction with PCNA
| Autor: | Marietta Y.W.T. Lee, Bin Xie, Amal Rahmeh, Yajing Zhou, Ernest Y.C. Lee, Hao Li |
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| Rok vydání: | 2011 |
| Předmět: |
DNA polymerase
viruses Protein subunit Amino Acid Motifs Molecular Sequence Data Down-Regulation dnaN Eukaryotic DNA replication Biochemistry DNA polymerase delta Proliferating Cell Nuclear Antigen Serine Humans Amino Acid Sequence Phosphorylation DNA Polymerase III Aspartic Acid DNA clamp biology Molecular Mimicry Processivity Cyclic AMP-Dependent Protein Kinases Molecular biology Proliferating cell nuclear antigen Cell biology Protein Subunits Mutation biology.protein Protein Processing Post-Translational HeLa Cells Protein Binding |
| Zdroj: | Biochemistry. 51:416-424 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi201638e |
| Popis: | DNA polymerase delta (Pol δ) is a central enzyme for eukaryotic DNA replication and repair. Pol δ is a complex of four subunits p125, p68, p50, and p12. The functional properties of Pol δ are largely determined by its interaction with its DNA sliding clamp PCNA (proliferating cellular nuclear antigen). The regulatory mechanisms that govern the association of Pol δ with PCNA are largely unknown. In this study, we identified S458, located in the PCNA-interacting protein (PIP-Box) motif of p68, as a phosphorylation site for PKA. Phosphomimetic mutation of S458 resulted in a decrease in p68 affinity for PCNA as well as the processivity of Pol δ. Our results suggest a role of phosphorylation of the PIP-motif of p68 as a molecular switch that dynamically regulates the functional properties of Pol δ. |
| Databáze: | OpenAIRE |
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