Journal
NUCLEIC ACIDS RESEARCH
Volume 41, Issue 9, Pages 4913-4925Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkt192
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Funding
- National Institutes of Health (NIH) [GM38559, GM58015]
- T32 training grant in Oncogenic Signals and Chromosome Biology [CA108459]
- NIH [GM58015]
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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 (delta) is capable of robust DNA synthesis at RAD51-mediated recombination intermediates dependent on the processivity clamp PCNA. Translesion synthesis polymerase eta (eta) 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 delta performs recombination-associated DNA synthesis, with translesion synthesis polymerases providing a supportive role as in normal replication.
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