ArticleProceedings of the National Academy of Sciences of the United States of America2009
A model for DNA polymerase switching involving a single cleft and the rim of the sliding clamp.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 84 citations in OpenAlex.
- The RecBCD complex interacts directly with the DNA sliding clamp in Escherichia coli.Nucleic acids research · 2026Article
- Functional asymmetry in processivity clamp proteins.Biophysical journal · 2025Review
- A bipartite interaction with the processivity clamp potentiates Pol IV-mediated TLS.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Topology and functional characterization of major outer membrane proteins of Treponema maltophilum and Treponema lecithinolyticum.Molecular oral microbiology · 2025Article
- Transposition with Tn3-family elements occurs through interaction with the host β-sliding clamp processivity factor.Nucleic acids research · 2024Article
- A bipartite interaction with the processivity clamp potentiates Pol IV-mediated TLS.bioRxiv : the preprint server for biology · 2024Article
- Thumb-domain dynamics modulate the functional repertoire of DNA-Polymerase IV (DinB).Nucleic acids research · 2023Article
- Direct visualization of translesion DNA synthesis polymerase IV at the replisome.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Compartmentalization of the replication fork by single-stranded DNA-binding protein regulates translesion synthesis.Nature structural & molecular biology · 2022Article
- During Translesion Synthesis, Escherichia coli DinB89 (T120P) Alters Interactions of DinB (Pol IV) with Pol III Subunit Assemblies and SSB, but Not with the β Clamp.Journal of bacteriology · 2022Article
- The methylation-independent mismatch repair machinery inMicrobiology (Reading, England) · 2021Review
- The Mutant βJournal of bacteriology · 2021Article
- Elevated Levels of the Escherichia coliJournal of bacteriology · 2021Article
- A gatekeeping function of the replicative polymerase controls pathway choice in the resolution of lesion-stalled replisomes.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Dynamics of the E. coli β-Clamp Dimer Interface and Its Influence on DNA Loading.Biophysical journal · 2019Article
- Binding of the regulatory domain of MutL to the sliding β-clamp is species specific.Nucleic acids research · 2019Article
- Investigation of sliding DNA clamp dynamics by single-molecule fluorescence, mass spectrometry and structure-based modeling.Nucleic acids research · 2018Article
- Single-molecule imaging reveals multiple pathways for the recruitment of translesion polymerases after DNA damage.Nature communications · 2017Article
- Single-molecule studies contrast ordered DNA replication with stochastic translesion synthesis.eLife · 2017Article
- Collision with duplex DNA renders Escherichia coli DNA polymerase III holoenzyme susceptible to DNA polymerase IV-mediated polymerase switching on the sliding clamp.Scientific reports · 2017Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The actions of Escherichia coli DNA Polymerase IV (Pol IV) in mutagenesis are managed by its interaction with the beta sliding clamp. In the structure reported by Bunting et al. [EMBO J (2003) 22:5883-5892], the C-tail of Pol IV contacts a hydrophobic cleft on the clamp, while residues V303-P305 reach over the dimer interface to contact the rim of the adjacent clamp protomer. Using mutant forms of these proteins impaired for either the rim or the cleft contacts, we determined that the rim contact was dispensable for Pol IV replication in vitro, while the cleft contact was absolutely required. Using an in vitro assay to monitor Pol III*-Pol IV switching, we determined that a single cleft on the clamp was sufficient to support the switch, and that both the rim and cleft contacts were required. Results from genetic experiments support a role for the cleft and rim contacts in Pol IV function in vivo. Taken together, our findings challenge the toolbelt model and suggest instead that Pol IV contacts the rim of the clamp adjacent to the cleft that is bound by Pol III* before gaining control of the same cleft that is bound by Pol III*.
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