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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

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 - 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 the exposed tetrad of a parallel-stranded G-quadruplex. The RHAU peptide folds into an L-shaped α-helix, and binds to the 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.
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https://hal-polytechnique.archives-ouvertes.fr/hal-02355168
Contributor : Aurélien Arnoux <>
Submitted on : Friday, November 8, 2019 - 10:22:32 AM
Last modification on : Wednesday, July 29, 2020 - 4:19:42 PM

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Brahim Heddi, Vee Vee Cheong, Emmanuelle Schmitt, Yves Mechulam, Anh Tuân Phan. 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, Elsevier, 2020, 209 (1), pp.S1047-8477(19)30210-2. ⟨10.1016/j.jsb.2019.10.001⟩. ⟨hal-02355168⟩

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