Journal
NUCLEIC ACIDS RESEARCH
Volume 42, Issue 13, Pages 8461-U177Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku547
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Funding
- KAKENHI from the Japan Society for the Promotion of Science and the Ministry of Education, Culture, Sports, Science and Technology, Japan [21870023, 25840009, 25291077, 25131713]
- LIGUE Contre le Cancer
- ANR ForkRepair [ANR 11 BSV8 017 01]
- United States Public Health Services Grant [R01ES003775]
- Grants-in-Aid for Scientific Research [25840009, 21870023, 25440009] Funding Source: KAKEN
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Escherichia coli DNA polymerase IV (Pol IV, also known as DinB) is a Y-family DNA polymerase capable of catalyzing translesion DNA synthesis (TLS) on certain DNA lesions, and accumulating data suggest that Pol IV may play an important role in copying various kinds of spontaneous DNA damage including N-2-dG adducts and alkylated bases. Pol IV has a unique ability to coexist with Pol III on the same beta clamp and to positively dissociate Pol III from beta clamp in a concentration-dependent manner. Reconstituting the entire process of TLS in vitro using E. coli replication machinery and Pol IV, we observed that a replication fork stalled at (-)-trans-anti-benzo[a]pyrene-N-2-dG lesion on the leading strand was efficiently and quickly recovered via two sequential switches from Pol III to Pol IV and back to Pol III. Our results suggest that TLS by Pol IV smoothes the way for the replication fork with minimal interruption.
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