期刊
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
卷 83, 期 4, 页码 695-704出版社
TAYLOR & FRANCIS LTD
DOI: 10.1080/09168451.2018.1559722
关键词
Archaea; DNA replication; RPA; replication fork progression; DNA polymerase
类别
资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan [JP26242075, JP18K05442]
- Japan Society for the Promotion of Science [JP16J02633]
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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