Why Two? On the Role of (A-)Symmetry in Negative Supercoiling of DNA by Gyrase

International Journal of Molecular Sciences
Dagmar Klostermeier

Abstract

Gyrase is a type IIA topoisomerase that catalyzes negative supercoiling of DNA. The enzyme consists of two GyrA and two GyrB subunits. It is believed to introduce negative supercoils into DNA by converting a positive DNA node into a negative node through strand passage: First, it cleaves both DNA strands of a double-stranded DNA, termed the G-segment, and then it passes a second segment of the same DNA molecule, termed the T-segment, through the gap created. As a two-fold symmetric enzyme, gyrase contains two copies of all elements that are key for the supercoiling reaction: The GyrB subunits provide two active sites for ATP binding and hydrolysis. The GyrA subunits contain two C-terminal domains (CTDs) for DNA binding and wrapping to stabilize the positive DNA node, and two catalytic tyrosines for DNA cleavage. While the presence of two catalytic tyrosines has been ascribed to the necessity of cleaving both strands of the G-segment to enable strand passage, the role of the two ATP hydrolysis events and of the two CTDs has been less clear. This review summarizes recent results on the role of these duplicate elements for individual steps of the supercoiling reaction, and discusses the implications for the mechanism of DNA superc...Continue Reading

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Citations

Jul 6, 2019·Nucleic Acids Research·Jorge B SchvartzmanAndrzej Stasiak
Jan 19, 2020·The Journal of Biological Chemistry·Daniela Weidlich, Dagmar Klostermeier
Mar 20, 2020·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Ana-Mădălina MăciucăValentina Uivarosi
Feb 26, 2019·Microbial Biotechnology·Grégory BoëlAntoine Danchin
Oct 30, 2019·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Eman M Mohi El-DeenEman S Nossier
Jan 27, 2021·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·Isaac Kyei Barffour, Desmond Omane Acheampong
Mar 7, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Dagmar Klostermeier
Apr 28, 2021·Nucleic Acids Research·Jana Hirsch, Dagmar Klostermeier

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Methods Mentioned

BETA
FRET
tandem-affinity purification
tandem-affinity
footprinting

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