RNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36

Ramreddy Tippana; Michael C. Chen; Natalia A. Demeshkina; Adrian R. Ferré-D’Amaré; Sua Myong

doi:10.1038/s41467-019-09802-w

Nature Communications (Apr 2019)

RNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36

Ramreddy Tippana,
Michael C. Chen,
Natalia A. Demeshkina,
Adrian R. Ferré-D’Amaré,
Sua Myong

Affiliations

Ramreddy Tippana: Department of Biophysics, Johns Hopkins University
Michael C. Chen: Department of Chemistry, University of Cambridge
Natalia A. Demeshkina: Biochemistry and Biophysics Center, National Heart, Lung and Blood Institute
Adrian R. Ferré-D’Amaré: Biochemistry and Biophysics Center, National Heart, Lung and Blood Institute
Sua Myong: Department of Biophysics, Johns Hopkins University

DOI: https://doi.org/10.1038/s41467-019-09802-w
Journal volume & issue: Vol. 10, no. 1
pp. 1 – 10

Abstract

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DHX36 is a G-quadruplex (G4) resolving helicase that targets both DNA-G4 and RNA-G4. Here the authors use single molecule FRET measurements and show that DHX36 resolves RNA-G4 structures by a mechanism involving an ATP-dependent, highly repetitive and stepwise refolding of RNA-G4 that differs from its DNA-G4 structures resolving mechanism.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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