RNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36
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 i...
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2019-04-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-019-09802-w |
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doaj-647ccd90166c47d89791e381e1f5cdef2021-05-11T11:46:45ZengNature Publishing GroupNature Communications2041-17232019-04-0110111010.1038/s41467-019-09802-wRNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36Ramreddy Tippana0Michael C. Chen1Natalia A. Demeshkina2Adrian R. Ferré-D’Amaré3Sua Myong4Department of Biophysics, Johns Hopkins UniversityDepartment of Chemistry, University of CambridgeBiochemistry and Biophysics Center, National Heart, Lung and Blood InstituteBiochemistry and Biophysics Center, National Heart, Lung and Blood InstituteDepartment of Biophysics, Johns Hopkins UniversityDHX36 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.https://doi.org/10.1038/s41467-019-09802-w |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Ramreddy Tippana Michael C. Chen Natalia A. Demeshkina Adrian R. Ferré-D’Amaré Sua Myong |
spellingShingle |
Ramreddy Tippana Michael C. Chen Natalia A. Demeshkina Adrian R. Ferré-D’Amaré Sua Myong RNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36 Nature Communications |
author_facet |
Ramreddy Tippana Michael C. Chen Natalia A. Demeshkina Adrian R. Ferré-D’Amaré Sua Myong |
author_sort |
Ramreddy Tippana |
title |
RNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36 |
title_short |
RNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36 |
title_full |
RNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36 |
title_fullStr |
RNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36 |
title_full_unstemmed |
RNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36 |
title_sort |
rna g-quadruplex is resolved by repetitive and atp-dependent mechanism of dhx36 |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2019-04-01 |
description |
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. |
url |
https://doi.org/10.1038/s41467-019-09802-w |
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1721445957652971520 |