Journal
MOLECULAR CELL
Volume 26, Issue 6, Pages 781-793Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2007.05.012
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Funding
- NIAID NIH HHS [R01 AI059027, AI059027] Funding Source: Medline
- NIGMS NIH HHS [GM073495, F32 GM073495-03, F32 GM073495, R01 GM068061, R01 GM068061-05] Funding Source: Medline
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Collapsed DNA replication forks must be reactivated through origin-independent reloading of the replication machinery (replisome) to ensure complete duplication of cellular genomes. In E. coli, the PriA-dependent pathway is the major replication restart mechanism and requires primosome proteins PriA, PriB, and DnaT for replisome reloading. However, the molecular mechanisms that regulate origin-independent replisome loading are not fully understood. Here, we demonstrate that assembly of primosome protein complexes represents a key regulatory mechanism, as inherently weak PriA-PriB and PriB-DnaT interactions are strongly stimulated by single-stranded DNA. Furthermore, the binding site on PriB for single-stranded DNA partially overlaps the binding sites for PriA and DnaT, suggesting a dynamic primosome assembly process in which single-stranded DNA is handed off from one primosome protein to another as a repaired replication fork is reactivated. This model helps explain how origin-independent initiation of DNA replication is restricted to repaired replication forks, preventing overreplication of the genome.
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