Reconstitution of recombination-associated DNA synthesis with human proteins Journal Article
| Authors: | Sneeden, J. L.; Grossi, S. M.; Tappin, I.; Hurwitz, J.; Heyer, W. D. |
| Article Title: | Reconstitution of recombination-associated DNA synthesis with human proteins |
| Abstract: | The repair of DNA breaks by homologous recombination is a high-fidelity process, necessary for the maintenance of genome integrity. Thus, DNA synthesis associated with recombinational repair must be largely error-free. In this report, we show that human DNA polymerase delta (δ) is capable of robust DNA synthesis at RAD51-mediated recombination intermediates dependent on the processivity clamp PCNA. Translesion synthesis polymerase eta (η) also extends these substrates, albeit far less processively. The single-stranded DNA binding protein RPA facilitates recombination-mediated DNA synthesis by increasing the efficiency of primer utilization, preventing polymerase stalling at specific sequence contexts, and overcoming polymerase stalling caused by topological constraint allowing the transition to a migrating D-loop. Our results support a model whereby the high-fidelity replicative DNA polymerase δ performs recombination-associated DNA synthesis, with translesion synthesis polymerases providing a supportive role as in normal replication. © 2013 The Author(s). |
| Journal Title: | Nucleic Acids Research |
| Volume: | 41 |
| Issue: | 9 |
| ISSN: | 0305-1048 |
| Publisher: | Oxford University Press |
| Date Published: | 2013-05-01 |
| Start Page: | 4913 |
| End Page: | 4925 |
| Language: | English |
| DOI: | 10.1093/nar/gkt192 |
| PROVIDER: | scopus |
| PMCID: | PMC3643601 |
| PUBMED: | 23535143 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 3 June 2013" - "CODEN: NARHA" - "Source: Scopus" |
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