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Updated: Jan 31, 2026

Kinetics of Lagging-strand DNA Synthesis In Vitro by the Bacteriophage T7 Replication Proteins
Published on: February 25, 2017
Replication protein A complex in Thermococcus kodakarensis interacts with DNA polymerases and helps their effective
Mariko Nagata1, Sonoko Ishino1, Takeshi Yamagami1
1a Department of Bioscience and Biotechnology, Graduate School of Bioresource and Bioenvironmental Sciences , Kyushu University , Fukuoka , Japan.
Abstract:
Replication protein A (RPA) is an essential component of DNA metabolic processes. RPA binds to single-stranded DNA (ssDNA) and interacts with multiple DNA-binding proteins. In this study, we showed that two DNA polymerases, PolB and PolD, from the hyperthermophilic archaeon Thermococcus kodakarensis interact directly with RPA in vitro. RPA was expected to play a role in resolving the secondary structure, which may stop the DNA synthesis reaction, in the template ssDNA. Our in vitro DNA synthesis assay showed that the pausing was resolved by RPA for both PolB and PolD. These results supported the fact that RPA interacts with DNA polymerases as a member of the replisome and is involved in the normal progression of DNA replication forks.
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