Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/150541
Title: Recognition of different base tetrads by RHAU (DHX36) : X-ray crystal structure of the G4 recognition motif bound to the 3'-end tetrad of a DNA G-quadruplex
Authors: Heddi, Brahim
Cheong, Vee Vee
Schmitt, Emmanuelle
Mechulam, Yves
Phan, Anh Tuân
Keywords: Science::Biological sciences
Issue Date: 2019
Source: Heddi, B., Cheong, V. V., Schmitt, E., Mechulam, Y. & Phan, A. T. (2019). Recognition of different base tetrads by RHAU (DHX36) : X-ray crystal structure of the G4 recognition motif bound to the 3'-end tetrad of a DNA G-quadruplex. Journal of Structural Biology, 209(1), 107399-. https://dx.doi.org/10.1016/j.jsb.2019.10.001
Project: MOE2018-T2-2-029
Journal: Journal of Structural Biology
Abstract: G-quadruplexes (G4) are secondary structures of nucleic acids that can form in cells and have diverse biological functions. Several biologically important proteins interact with G-quadruplexes, of which RHAU (or DHX36) - a helicase from the DEAH-box superfamily, was shown to bind and unwind G-quadruplexes efficiently. We report a X-ray co-crystal structure at 1.5 Å resolution of an N-terminal fragment of RHAU bound to an exposed tetrad of a parallel-stranded G-quadruplex. The RHAU peptide folds into an L-shaped α-helix, and binds to a G-quadruplex through π-stacking and electrostatic interactions. X-ray crystal structure of our complex identified key amino acid residues important for G-quadruplex-peptide binding interaction at the 3'-end G•G•G•G tetrad. Together with previous solution and crystal structures of RHAU bound to the 5'-end G•G•G•G and G•G•A•T tetrads, our crystal structure highlights the occurrence of a robust G-quadruplex recognition motif within RHAU that can adapt to different accessible tetrads.
URI: https://hdl.handle.net/10356/150541
ISSN: 1047-8477
DOI: 10.1016/j.jsb.2019.10.001
Rights: © 2019 Elsevier Inc. All rights reserved. This paper was published in Journal of Structural Biology and is made available with permission of Elsevier Inc.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SPMS Journal Articles

Page view(s)

29
Updated on Jul 27, 2021

Download(s) 50

19
Updated on Jul 27, 2021

Google ScholarTM

Check

Altmetric


Plumx

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.