PMID:23260658
| Citation |
Lia, G, Rigato, A, Long, E, Chagneau, C, Le Masson, M, Allemand, JF and Michel, B (2013) RecA-promoted, RecFOR-independent progressive disassembly of replisomes stalled by helicase inactivation. Mol. Cell 49:547-57 |
|---|---|
| Abstract |
In all organisms, replication impairment is a recognized source of genomic instability, raising an increasing interest in the fate of inactivated replication forks. We used Escherichia coli strains with a temperature-inactivated replicative helicase (DnaB) and in vivo single-molecule microscopy to quantify the detailed molecular processing of stalled replication forks. After helicase inactivation, RecA binds to blocked replication forks and is essential for the rapid release of hPol III. The entire holoenzyme is disrupted little by little, with some components lost in few minutes, while others are stable in 70% of cells for at least 1 hr. Although replisome dissociation is delayed in a recA mutant, it is not affected by RecF or RecO inactivation. RecFOR are required for full RecA filaments formation, and we propose that polymerase clearance can be catalyzed by short, RecFOR-independent RecA filaments. Our results identify a function for the universally conserved, central recombination protein RecA. |
| Links |
PubMed Online version:10.1016/j.molcel.2012.11.018 |
| Keywords |
DNA Polymerase III/metabolism; DNA Replication; DNA, Bacterial/metabolism; DNA-Binding Proteins/metabolism; DNA-Directed DNA Polymerase/metabolism; DnaB Helicases/metabolism; Enzyme Activation; Escherichia coli/cytology; Escherichia coli/enzymology; Escherichia coli Proteins/metabolism; Fluorescence; Holoenzymes/metabolism; Luminescent Proteins/metabolism; Multienzyme Complexes/metabolism; Protein Binding; Rec A Recombinases/metabolism; Temperature |
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