ArticleNucleic acids research2009
Contributions of the individual hydrophobic clefts of the Escherichia coli beta sliding clamp to clamp loading, DNA replication and clamp recycling.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- The loop domains of the E. coli β sliding clamp are required for Hda-dependent inactivation of DnaA.Genetics · 2026Article
- Functional asymmetry in processivity clamp proteins.Biophysical journal · 2025Review
- Escherichia coli DNA replication: the old model organism still holds many surprises.FEMS microbiology reviews · 2024Review
- The bacterial DNA sliding clamp, β-clamp: structure, interactions, dynamics and drug discovery.Cellular and molecular life sciences : CMLS · 2024Review
- 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 Mutant βJournal of bacteriology · 2021Article
- Elevated Levels of the Escherichia coliJournal of bacteriology · 2021Article
- Watching DNA Replication Inhibitors in Action: Exploiting Time-Lapse Microfluidic Microscopy as a Tool for Target-Drug Interaction Studies inAntimicrobial agents and chemotherapy · 2019Article
- Dynamics of the E. coli β-Clamp Dimer Interface and Its Influence on DNA Loading.Biophysical journal · 2019Article
- Exchange between Escherichia coli polymerases II and III on a processivity clamp.Nucleic acids research · 2016Article
- The β2 clamp in the Mycobacterium tuberculosis DNA polymerase III αβ2ε replicase promotes polymerization and reduces exonuclease activity.Scientific reports · 2016Article
- A Genetic Selection for dinB Mutants Reveals an Interaction between DNA Polymerase IV and the Replicative Polymerase That Is Required for Translesion Synthesis.PLoS genetics · 2015Article
- Polymerase exchange on single DNA molecules reveals processivity clamp control of translesion synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- A direct proofreader-clamp interaction stabilizes the Pol III replicase in the polymerization mode.The EMBO journal · 2013Article
- Architecture of the Pol III-clamp-exonuclease complex reveals key roles of the exonuclease subunit in processive DNA synthesis and repair.The EMBO journal · 2013Article
- Escherichia coli DNA polymerase IV (Pol IV), but not Pol II, dynamically switches with a stalled Pol III* replicase.Journal of bacteriology · 2012Article
- Escherichia coli processivity clamp β from DNA polymerase III is dynamic in solution.Biochemistry · 2011Article
- A single hydrophobic cleft in the Escherichia coli processivity clamp is sufficient to support cell viability and DNA damage-induced mutagenesis in vivo.BMC molecular biology · 2010Article
- The Roles of UmuD in Regulating Mutagenesis.Journal of nucleic acids · 2010Article
- Mutations in the Bacillus subtilis beta clamp that separate its roles in DNA replication from mismatch repair.Journal of bacteriology · 2010Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
The homodimeric Escherichia coli beta sliding clamp contains two hydrophobic clefts with which proteins involved in DNA replication, repair and damage tolerance interact. Deletion of the C-terminal five residues of beta (beta(C)) disrupted both clefts, severely impairing interactions of the clamp with the DnaX clamp loader, as well as the replicative DNA polymerase, Pol III. In order to determine whether both clefts were required for loading clamp onto DNA, stimulation of Pol III replication and removal of clamp from DNA after replication was complete, we developed a method for purification of heterodimeric clamp proteins comprised of one wild-type subunit (beta(+)), and one beta(C) subunit (beta(+)/beta(C)). The beta(+)/beta(C) heterodimer interacted normally with the DnaX clamp loader, and was loaded onto DNA slightly more efficiently than was beta(+). Moreover, beta(+)/beta(C) interacted normally with Pol III, and stimulated replication to the same extent as did beta(+). Finally, beta(+)/beta(C) was severely impaired for unloading from DNA using either DnaX or the delta subunit of DnaX. Taken together, these findings indicate that a single cleft in the beta clamp is sufficient for both loading and stimulation of Pol III replication, but both clefts are required for unloading clamp from DNA after replication is completed.
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