TY - JOUR
T1 - Replication protein A complex in Thermococcus kodakarensis interacts with DNA polymerases and helps their effective strand synthesis
AU - Nagata, Mariko
AU - Ishino, Sonoko
AU - Yamagami, Takeshi
AU - Ishino, Yoshizumi
N1 - Funding Information:
This work was supported by <Ministry of Education, Culture, Sports, Science and Technology of Japan>, [JP26242075 to Y.I., and JP18K05442 to S.I.], and a <Grant-in-Aid from the Japan Society for the Promotion of Science Fellows>, [JP16J02633 to M.N.].
Publisher Copyright:
© 2018 Informa UK Limited, trading as Taylor & Francis Group.
PY - 2019
Y1 - 2019
N2 - 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.
AB - 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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U2 - 10.1080/09168451.2018.1559722
DO - 10.1080/09168451.2018.1559722
M3 - Article
C2 - 30582424
AN - SCOPUS:85063611320
SN - 0916-8451
VL - 83
SP - 695
EP - 704
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 4
ER -