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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


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Volume 395, Issue 1

Issues

Differential contributions of the latch in Thermotoga maritima reverse gyrase to the binding of single-stranded DNA before and after ATP hydrolysis

Yoandris del Toro Duany
  • Institute for Physical Chemistry, University of Münster, Corrensstrasse 30, D-48149 Münster, Germany
  • Present address: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Agneyo Ganguly
  • Institute for Physical Chemistry, University of Münster, Corrensstrasse 30, D-48149 Münster, Germany
  • Present address: Department of Biotechnology, Presidency University, 86/1 College Street, Kolkata 700073, India
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Dagmar Klostermeier
  • Corresponding author
  • Institute for Physical Chemistry, University of Münster, Corrensstrasse 30, D-48149 Münster, Germany
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2013-08-16 | DOI: https://doi.org/10.1515/hsz-2013-0177

Abstract

Reverse gyrase catalyzes the ATP-dependent introduction of positive supercoils into DNA. Supercoiling requires the functional cooperation of its N-terminal helicase domain with the C-terminal topoisomerase domain. The helicase domain contains a superfamily 2 helicase core formed by two RecA domains, H1 and H2. We show here that a helicase domain lacking the latch, an insertion in H2, fails to close the cleft in the helicase core in response to nucleotide and DNA binding at the beginning of the catalytic cycle. In the presence of the pre-hydrolysis ATP analog ADP·BeFx, however, the closed conformer can still be formed in the absence of the latch. The helicase domain lacking the latch exhibits reduced DNA affinities. The energetic difference between the two nucleotide states involved in duplex separation is diminished, rationalizing the unwinding deficiency of reverse gyrase lacking the latch. The latch most strongly contributes to binding of single-stranded DNA in the post-hydrolysis state, before phosphate release. Our results are in line with contributions of the latch in determining the direction of strand passage, and in orienting the cleaved single-stranded DNA for re-ligation. At the same time, the latch may coordinate the re-ligation reaction with strand passage and with the nucleotide cycle.

This article offers supplementary material which is provided at the end of the article.

Keywords: DNA unwinding; helicase; latch; nucleotide cycle; positive supercoiling; topoisomerase

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About the article

Corresponding author: Dagmar Klostermeier, Institute for Physical Chemistry, University of Münster, Corrensstrasse 30, D-48149 Münster, Germany, e-mail:


Received: 2013-05-13

Accepted: 2013-08-14

Published Online: 2013-08-16

Published in Print: 2014-01-01


Citation Information: Biological Chemistry, Volume 395, Issue 1, Pages 83–93, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2013-0177.

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