Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 108, Issue 18, Pages 7419-7424Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1018436108
Keywords
DNA topology; protein-DNA interactions; single-DNA biophysics; site-specific recombination
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Funding
- National Science Foundation [DMR-0715099, PHY-0852130]
- Chicago Biomedical Consortium with Chicago Community Trust
- National Institutes of Health (NIH)-National Cancer Institute (NCI) [U54CA143869-01]
- NIH [GM028470, AI059114]
- Yale University
- Division Of Physics
- Direct For Mathematical & Physical Scien [0852130] Funding Source: National Science Foundation
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DNA recombinases exchange duplex DNAs by rigid-body relative rotation of the two halves of the synapse, mediated by a flat protein-protein interaction surface. We present evidence for this rotational motion for a simple serine recombinase, the Bxb1 phage integrase, from a single-DNA-based supercoil-release assay that allows us to follow crossover site cleavage, rotation, religation, and product release in real time. We have also used a two-DNA braiding-relaxation experiment to observe the effect of synapse rotation in reactions on two long molecules. Relaxation and un-braiding are rapid (averaging 54 and 70 turns/s, respectively) and complete, with no discernible pauses. Nevertheless, the molecular friction associated with rotation is larger than that of type-I topoisomerases in a similar assay. Surprisingly we find that the synapse can stay rotationally open for many minutes.
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