Back to Search
Start Over
A structural model of the PriB-DnaT complex in Escherichia coli replication restart.
- Source :
-
FEBS letters [FEBS Lett] 2021 Feb; Vol. 595 (3), pp. 341-350. Date of Electronic Publication: 2020 Dec 13. - Publication Year :
- 2021
-
Abstract
- 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.<br /> (© 2020 Federation of European Biochemical Societies.)
- Subjects :
- Binding Sites
DNA Replication
DNA, Bacterial genetics
DNA, Bacterial metabolism
DNA, Single-Stranded genetics
DNA, Single-Stranded metabolism
DNA-Binding Proteins genetics
DNA-Binding Proteins metabolism
Escherichia coli metabolism
Escherichia coli Proteins genetics
Escherichia coli Proteins metabolism
Genetic Complementation Test
Molecular Dynamics Simulation
Mutation
Peptides chemistry
Peptides genetics
Peptides metabolism
Plasmids chemistry
Plasmids metabolism
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Thermodynamics
DNA, Bacterial chemistry
DNA, Single-Stranded chemistry
DNA-Binding Proteins chemistry
Escherichia coli genetics
Escherichia coli Proteins chemistry
Gene Expression Regulation, Bacterial
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 595
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 33275781
- Full Text :
- https://doi.org/10.1002/1873-3468.14020