TY - JOUR
T1 - A structural model of the PriB–DnaT complex in Escherichia coli replication restart
AU - Abe, Yoshito
AU - Ikeda, Yohei
AU - Fujiyama, Saki
AU - Kini, R. Manjunatha
AU - Ueda, Tadashi
N1 - Funding Information:
This work was supported by Grant-in-Aid for JSPS Research Fellow for SF and by JSPS KAKENHI Grant Number JP26440031 for YA. We are grateful to Prof. Steven J. Sandler of University of Massachusetts at Amherst for the kind gift of sample and to his laboratory student Anastasiia Klimova for her help. And we thank Prof. Cho Yeow Koh of National University of Singapore for his help of peptide synthesis. We also thank KN International for improving the English usage in the manuscript.
Funding Information:
This work was supported by Grant‐in‐Aid for JSPS Research Fellow for SF and by JSPS KAKENHI Grant Number JP26440031 for YA.
Publisher Copyright:
© 2020 Federation of European Biochemical Societies
PY - 2021/2
Y1 - 2021/2
N2 - In Escherichia coli, DNA replication is restarted following DNA repair by the PriA-dependent pathway, in which the binding and dissociation of proteins such as PriA, PriB, and DnaT on ssDNA lead to the formation of a protein–DNA complex for recruiting the DnaB–DnaC replication protein complex. However, the structure of the PriB–DnaT complex, which is an essential step in the PriA-dependent pathway, remains elusive. In this study, the importance of His26 in PriB for replication restart was reconfirmed using plasmid complementation. Furthermore, we used NMR to examine the DnaT interaction sites on PriB. We also evaluated the PriB–DnaT peptide complex model, which was prepared by in silico docking, using molecular dynamic simulation. From these data, we propose a structural model that provides insight into the PriB–DnaT interaction.
AB - In Escherichia coli, DNA replication is restarted following DNA repair by the PriA-dependent pathway, in which the binding and dissociation of proteins such as PriA, PriB, and DnaT on ssDNA lead to the formation of a protein–DNA complex for recruiting the DnaB–DnaC replication protein complex. However, the structure of the PriB–DnaT complex, which is an essential step in the PriA-dependent pathway, remains elusive. In this study, the importance of His26 in PriB for replication restart was reconfirmed using plasmid complementation. Furthermore, we used NMR to examine the DnaT interaction sites on PriB. We also evaluated the PriB–DnaT peptide complex model, which was prepared by in silico docking, using molecular dynamic simulation. From these data, we propose a structural model that provides insight into the PriB–DnaT interaction.
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U2 - 10.1002/1873-3468.14020
DO - 10.1002/1873-3468.14020
M3 - Article
C2 - 33275781
AN - SCOPUS:85097497316
SN - 0014-5793
VL - 595
SP - 341
EP - 350
JO - FEBS Letters
JF - FEBS Letters
IS - 3
ER -