ArticleThe Journal of biological chemistry2013
The β sliding clamp closes around DNA prior to release by the Escherichia coli clamp loader γ complex.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Structural characterisation of the complete cycle of sliding clamp loading in Escherichia coli.Nature communications · 2024Article
- The bacterial DNA sliding clamp, β-clamp: structure, interactions, dynamics and drug discovery.Cellular and molecular life sciences : CMLS · 2024Review
- Differences between bacteria and eukaryotes in clamp loader mechanism, a conserved process underlying DNA replication.The Journal of biological chemistry · 2024Article
- Differences in clamp loader mechanism between bacteria and eukaryotes.bioRxiv : the preprint server for biology · 2023Article
- The Escherichia coli clamp loader rapidly remodels SSB on DNA to load clamps.Nucleic acids research · 2022Article
- Deep Analysis of Residue Constraints (DARC): identifying determinants of protein functional specificity.Scientific reports · 2020Article
- Escherichia coli β-clamp slows down DNA polymerase I dependent nick translation while accelerating ligation.PloS one · 2018Article
- Linchpin DNA-binding residues serve as go/no-go controls in the replication factor C-catalyzed clamp-loading mechanism.The Journal of biological chemistry · 2017Article
- Dynamics of Open DNA Sliding Clamps.PloS one · 2016Article
- Kinetic analysis of PCNA clamp binding and release in the clamp loading reaction catalyzed by Saccharomyces cerevisiae replication factor C.Biochimica et biophysica acta · 2015Article
- Slow unloading leads to DNA-bound β2-sliding clamp accumulation in live Escherichia coli cells.Nature communications · 2014Article
- Loading dynamics of a sliding DNA clamp.Angewandte Chemie (International ed. in English) · 2014Article
- The interplay of primer-template DNA phosphorylation status and single-stranded DNA binding proteins in directing clamp loaders to the appropriate polarity of DNA.Nucleic acids research · 2014Article
- Probing DNA clamps with single-molecule force spectroscopy.Nucleic acids research · 2013Article
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Authors and funding
2 authors.
Funding
Abstract
Escherichia coli γ complex clamp loader functions to load the β sliding clamp onto sites of DNA replication and repair. The clamp loader uses the energy of ATP binding and hydrolysis to drive conformational changes allowing for β binding and opening, DNA binding, and then release of the β·DNA complex. Although much work has been done studying the sliding clamp and clamp loader mechanism, kinetic analysis of the events following β·γ complex·DNA formation is not complete. Using fluorescent clamp closing and release assays, we show that β closing is faster than β release, indicating that γ complex closes β before releasing it around DNA. Using a fluorescent ATP hydrolysis assay, we show that there is a burst of ATP hydrolysis before β closing and that β release may be the rate-limiting step in the overall clamp loading reaction. The combined use of these fluorescent assays provides a unique perspective into the E. coli clamp loader by providing a measure of the relative timing of different events in the clamp loading reaction, helping to elucidate the complicated clamp loading mechanism.
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