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Updated: Aug 24, 2026

Studying DNA Looping by Single-Molecule FRET
Published on: June 28, 2014
Enzyme-mediated DNA looping
Stephen E Halford1, Abigail J Welsh, Mark D Szczelkun
1Department of Biochemistry, School of Medical Sciences, University of Bristol, University walk, Bristol BS8 1TD, United Kingdom. s.halford@bristol.ac.uk
Abstract:
Most reactions on DNA are carried out by multimeric protein complexes that interact with two or more sites in the DNA and thus loop out the DNA between the sites. The enzymes that catalyze these reactions usually have no activity until they interact with both sites. This review examines the mechanisms for the assembly of protein complexes spanning two DNA sites and the resultant triggering of enzyme activity. There are two main routes for bringing together distant DNA sites in an enzyme complex: either the proteins bind concurrently to both sites and capture the intervening DNA in a loop, or they translocate the DNA between one site and another into an expanding loop, by an energy-dependent translocation mechanism. Both capture and translocation mechanisms are discussed here, with reference to the various types of restriction endonuclease that interact with two recognition sites before cleaving DNA.
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