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A structural model of the PriB–DnaT complex in Escherichia coli replication restart
Author(s) -
Abe Yoshito,
Ikeda Yohei,
Fujiyama Saki,
Kini R. Manjunatha,
Ueda Tadashi
Publication year - 2021
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14020
Subject(s) - dna replication , escherichia coli , dna , in silico , chemistry , biology , biophysics , biochemistry , gene
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.