Potassium ions are required for nucleotide-induced closure of gyrase N-gate.

The Journal of Biological Chemistry
Airat Gubaev, Dagmar Klostermeier

Abstract

DNA gyrase catalyzes ATP-dependent negative supercoiling of DNA by a strand passage mechanism that requires coordinated opening and closing of three protein interfaces, the N-, DNA-, and C-gates. ATP binding to the GyrB subunits of gyrase causes dimerization and N-gate closure. The closure of the N-gate is a key step in the gyrase catalytic cycle, as it captures the DNA segment to be transported and poises gyrase toward strand passage. We show here that K(+) ions are required for DNA supercoiling but are dispensable for ATP-independent DNA relaxation. Although DNA binding, distortion, wrapping, and DNA-induced narrowing of the N-gate occur in the absence of K(+), nucleotide-induced N-gate closure depends on their presence. Our results provide evidence that K(+) ions relay small conformational changes in the nucleotide-binding pocket to the formation of a tight dimer interface at the N-gate by connecting regions from both GyrB monomers and suggest an important role for K(+) in synchronization of N-gate closure and DNA-gate opening.

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Citations

Feb 1, 2014·Journal of Infection and Chemotherapy : Official Journal of the Japan Society of Chemotherapy·Hisashi ShojiYoshihito Niki
Mar 27, 2016·Journal of Molecular Biology·Aakash BasuZev Bryant
Apr 8, 2015·Acta Crystallographica. Section D, Biological Crystallography·Stephen James HearnshawDavid Mark Lawson
Jan 19, 2020·The Journal of Biological Chemistry·Daniela Weidlich, Dagmar Klostermeier
May 19, 2018·International Journal of Molecular Sciences·Dagmar Klostermeier
Mar 7, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Dagmar Klostermeier

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