Publication

Analysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a novel interactor of cellular G-quadruplex containing transcripts

Herdy, B., Mayer, C., Varshney, D., Marsico, G., Murat, P., Taylor, C., D'Santos, C., Tannahill, D. & Balasubramanian, S., 30-Nov-2018, In : Nucleic Acids Research. 46, 21, p. 11592-11604 13 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Herdy, B., Mayer, C., Varshney, D., Marsico, G., Murat, P., Taylor, C., ... Balasubramanian, S. (2018). Analysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a novel interactor of cellular G-quadruplex containing transcripts. Nucleic Acids Research, 46(21), 11592-11604. https://doi.org/10.1093/nar/gky861

Author

Herdy, Barbara ; Mayer, Clemens ; Varshney, Dhaval ; Marsico, Giovanni ; Murat, Pierre ; Taylor, Chris ; D'Santos, Clive ; Tannahill, David ; Balasubramanian, Shankar. / Analysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a novel interactor of cellular G-quadruplex containing transcripts. In: Nucleic Acids Research. 2018 ; Vol. 46, No. 21. pp. 11592-11604.

Harvard

Herdy, B, Mayer, C, Varshney, D, Marsico, G, Murat, P, Taylor, C, D'Santos, C, Tannahill, D & Balasubramanian, S 2018, 'Analysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a novel interactor of cellular G-quadruplex containing transcripts' Nucleic Acids Research, vol. 46, no. 21, pp. 11592-11604. https://doi.org/10.1093/nar/gky861

Standard

Analysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a novel interactor of cellular G-quadruplex containing transcripts. / Herdy, Barbara; Mayer, Clemens; Varshney, Dhaval; Marsico, Giovanni; Murat, Pierre; Taylor, Chris; D'Santos, Clive; Tannahill, David; Balasubramanian, Shankar.

In: Nucleic Acids Research, Vol. 46, No. 21, 30.11.2018, p. 11592-11604.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Herdy B, Mayer C, Varshney D, Marsico G, Murat P, Taylor C et al. Analysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a novel interactor of cellular G-quadruplex containing transcripts. Nucleic Acids Research. 2018 Nov 30;46(21):11592-11604. https://doi.org/10.1093/nar/gky861


BibTeX

@article{71604105f3ab410197d94cf9cc4117f1,
title = "Analysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a novel interactor of cellular G-quadruplex containing transcripts",
abstract = "RNA G-quadruplexes (rG4s) are secondary structures in mRNAs known to influence RNA post-transcriptional mechanisms thereby impacting neurodegenerative disease and cancer. A detailed knowledge of rG4-protein interactions is vital to understand rG4 function. Herein, we describe a systematic affinity proteomics approach that identified 80 high-confidence interactors that assemble on the rG4 located in the 5'-untranslated region (UTR) of the NRAS oncogene. Novel rG4 interactors included DDX3X, DDX5, DDX17, GRSF1 and NSUN5. The majority of identified proteins contained a glycine-arginine (GAR) domain and notably GAR-domain mutation in DDX3X and DDX17 abrogated rG4 binding. Identification of DDX3X targets by transcriptome-wide individual-nucleotide resolution UV-crosslinking and affinity enrichment (iCLAE) revealed a striking association with 5'-UTR rG4-containing transcripts which was reduced upon GAR-domain mutation. Our work highlights hitherto unrecognized features of rG4 structure-protein interactions that highlight new roles of rG4 structures in mRNA post-transcriptional control.",
keywords = "DNA, TRANSLATION, CYTOSCAPE, IDENTIFICATION, COMPLEX, TARGET, 5'-UTR",
author = "Barbara Herdy and Clemens Mayer and Dhaval Varshney and Giovanni Marsico and Pierre Murat and Chris Taylor and Clive D'Santos and David Tannahill and Shankar Balasubramanian",
year = "2018",
month = "11",
day = "30",
doi = "10.1093/nar/gky861",
language = "English",
volume = "46",
pages = "11592--11604",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "21",

}

RIS

TY - JOUR

T1 - Analysis of NRAS RNA G-quadruplex binding proteins reveals DDX3X as a novel interactor of cellular G-quadruplex containing transcripts

AU - Herdy, Barbara

AU - Mayer, Clemens

AU - Varshney, Dhaval

AU - Marsico, Giovanni

AU - Murat, Pierre

AU - Taylor, Chris

AU - D'Santos, Clive

AU - Tannahill, David

AU - Balasubramanian, Shankar

PY - 2018/11/30

Y1 - 2018/11/30

N2 - RNA G-quadruplexes (rG4s) are secondary structures in mRNAs known to influence RNA post-transcriptional mechanisms thereby impacting neurodegenerative disease and cancer. A detailed knowledge of rG4-protein interactions is vital to understand rG4 function. Herein, we describe a systematic affinity proteomics approach that identified 80 high-confidence interactors that assemble on the rG4 located in the 5'-untranslated region (UTR) of the NRAS oncogene. Novel rG4 interactors included DDX3X, DDX5, DDX17, GRSF1 and NSUN5. The majority of identified proteins contained a glycine-arginine (GAR) domain and notably GAR-domain mutation in DDX3X and DDX17 abrogated rG4 binding. Identification of DDX3X targets by transcriptome-wide individual-nucleotide resolution UV-crosslinking and affinity enrichment (iCLAE) revealed a striking association with 5'-UTR rG4-containing transcripts which was reduced upon GAR-domain mutation. Our work highlights hitherto unrecognized features of rG4 structure-protein interactions that highlight new roles of rG4 structures in mRNA post-transcriptional control.

AB - RNA G-quadruplexes (rG4s) are secondary structures in mRNAs known to influence RNA post-transcriptional mechanisms thereby impacting neurodegenerative disease and cancer. A detailed knowledge of rG4-protein interactions is vital to understand rG4 function. Herein, we describe a systematic affinity proteomics approach that identified 80 high-confidence interactors that assemble on the rG4 located in the 5'-untranslated region (UTR) of the NRAS oncogene. Novel rG4 interactors included DDX3X, DDX5, DDX17, GRSF1 and NSUN5. The majority of identified proteins contained a glycine-arginine (GAR) domain and notably GAR-domain mutation in DDX3X and DDX17 abrogated rG4 binding. Identification of DDX3X targets by transcriptome-wide individual-nucleotide resolution UV-crosslinking and affinity enrichment (iCLAE) revealed a striking association with 5'-UTR rG4-containing transcripts which was reduced upon GAR-domain mutation. Our work highlights hitherto unrecognized features of rG4 structure-protein interactions that highlight new roles of rG4 structures in mRNA post-transcriptional control.

KW - DNA

KW - TRANSLATION

KW - CYTOSCAPE

KW - IDENTIFICATION

KW - COMPLEX

KW - TARGET

KW - 5'-UTR

U2 - 10.1093/nar/gky861

DO - 10.1093/nar/gky861

M3 - Article

VL - 46

SP - 11592

EP - 11604

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 21

ER -

ID: 76693712