ArticleAngewandte Chemie (International ed. in English)2014
Loading dynamics of a sliding DNA clamp.
Article in Angewandte Chemie (International ed. in English), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Review of FRET biosensing and its application in biomolecular detection.American journal of translational research · 2023Review
- Kinetic Modeling of the Genetic Information Processes in a Minimal Cell.Frontiers in molecular biosciences · 2019Article
- Watching cellular machinery in action, one molecule at a time.The Journal of cell biology · 2017Review
- Dynamics of Open DNA Sliding Clamps.PloS one · 2016Article
- Replisome Assembly at Bacterial Chromosomes and Iteron Plasmids.Frontiers in molecular biosciences · 2016Review
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Sliding DNA clamps are loaded at a ss/dsDNA junction by a clamp loader that depends on ATP binding for clamp opening. Sequential ATP hydrolysis results in closure of the clamp so that it completely encircles and diffuses on dsDNA. We followed events during loading of an E. coli β clamp in real time by using single-molecule FRET (smFRET). Three successive FRET states were retained for 0.3 s, 0.7 s, and 9 min: Hydrolysis of the first ATP molecule by the γ clamp loader resulted in closure of the clamp in 0.3 s, and after 0.7 s in the closed conformation, the clamp was released to diffuse on the dsDNA for at least 9 min. An additional single-molecule polarization study revealed that the interfacial domain of the clamp rotated in plane by approximately 8° during clamp closure. The single-molecule polarization and FRET studies thus revealed the real-time dynamics of the ATP-hydrolysis-dependent 3D conformational change of the β clamp during loading at a ss/dsDNA junction.
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