Replication fork binding triggers structural changes in the PriA helicase that govern DNA replication restart in E. coli

Author:

Duckworth Alexander T.ORCID,Ducos Peter L.ORCID,McMillan Sarah D.ORCID,Satyshur Kenneth A.ORCID,Blumenthal Katelien H.,Deorio Haley R.ORCID,Larson Joseph A.ORCID,Sandler Steven J.ORCID,Grant TimothyORCID,Keck James L.ORCID

Abstract

AbstractBacterial replisomes often dissociate from replication forks before chromosomal replication is complete. To avoid the lethal consequences of such situations, bacteria have evolved replication restart pathways that reload replisomes onto prematurely terminated replication forks. To understand how the primary replication restart pathway in E. coli (PriA-PriB) selectively acts on replication forks, we determined the cryogenic-electron microscopy structure of a PriA/PriB/replication fork complex. Replication fork specificity arises from extensive PriA interactions with each arm of the branched DNA. These interactions reshape the PriA protein to create a pore encircling single-stranded lagging-strand DNA while also exposing a surface of PriA onto which PriB docks. Together with supporting biochemical and genetic studies, the structure reveals a switch-like mechanism for replication restart initiation in which restructuring of PriA directly couples replication fork recognition to PriA/PriB complex formation to ensure robust and high-fidelity replication re-initiation.

Funder

U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry,Multidisciplinary

Cited by 1 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Oligomeric state of the N-terminal domain of DnaT for replication restart in Escherichia coli;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2023-09

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