Identification of Subunit Binding Positions on a Model Fork and Displacements That Occur during Sequential Assembly of the Escherichia coli Primosome.

The Journal of Biological Chemistry
Carol M Manhart, Charles S McHenry

Abstract

When replication stalls and forks disassemble, the restart primosome is required to reload the replicative helicase so that chromosomal replication can be reinitiated. We have taken a photo-cross-linking approach, using model replication forks containing a phenyl diazirine placed at single locations, to determine the positions of primosomal protein binding and changes in interactions that occur during the assembly reaction. This approach revealed a novel mode for single-stranded DNA-binding protein (SSB)-DNA binding, in which SSB interacts with both the leading and lagging single-strand segments and the parental duplex of the fork. Cross-linking to a novel region within SSB is observed only when it is bound to forked structures. This binding mode is also followed by PriB. PriA binds to the fork, excluding SSB and PriB, interacting with the primer terminus, single-stranded leading and lagging strands and duplex in immediate proximity of the fork. SSB binds to flanking single-stranded segments distal to the fork in the presence of PriA. The addition of PriB or DnaT to a PriA-SSB-fork complex does not lead to cross-linking or displacement, suggesting that their association is through protein-protein interactions at early stages of...Continue Reading

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Citations

Aug 4, 2016·Nucleic Acids Research·Tricia A Windgassen, James L Keck
Dec 5, 2017·Nucleic Acids Research·Tricia A WindgassenJames L Keck
Sep 25, 2017·The Journal of Biological Chemistry·Sean M CarneyMichael A Trakselis
Nov 19, 2015·Nucleic Acids Research·Ivana Ivančić-BaćeEdward L Bolt
Sep 12, 2018·Proceedings of the National Academy of Sciences of the United States of America·Tricia A WindgassenJames L Keck
Aug 24, 2021·Molecular Microbiology·Steven J SandlerJames L Keck
Dec 25, 2021·Nucleic Acids Research·Phuong PhamMyron F Goodman

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