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Nat Struct Mol Biol. 2017 May;24(5):484-490. doi: 10.1038/nsmb.3401. Epub 2017 Apr 17.

An orthogonal single-molecule experiment reveals multiple-attempt dynamics of type IA topoisomerases.

Author information

1
Department of Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.
2
Department of Physics and Astronomy, Northwestern University, Evanston, Illinois, USA.

Abstract

Topoisomerases are enzymes that are involved in maintaining the topological state of cellular DNA. Their dynamic characteristics remain poorly understood despite numerous structural, biophysical and biochemical studies. Recent single-molecule experiments revealed that an important feature of the type IA topoisomerase mechanism is the presence of pauses between relaxation events. However, these experiments could not determine whether the protein remains DNA bound during the pauses or what relationship may exist between protein domain movements and topological changes in the DNA. By combining two orthogonal single-molecule techniques, we found that E. coli topoisomerase I constantly changes conformation when attempting to modify the topology of DNA, but succeeds in only a fraction of the attempts. Thus, its mechanism can be described as a series of DNA strand-passage attempts that culminate in a successful relaxation event.

PMID:
28414321
PMCID:
PMC5516274
DOI:
10.1038/nsmb.3401
[Indexed for MEDLINE]
Free PMC Article

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