期刊
NUCLEIC ACIDS RESEARCH
卷 46, 期 21, 页码 11592-11604出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gky861
关键词
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资金
- ERC [339778]
- Cancer Research UK [C14303/A17197]
- Marie Sklodowska-Curie Actions Individual Fellowship [702476]
- Swiss National Science Foundation [P2EZP2 152216]
- Marie Curie Actions (MSCA) [702476] Funding Source: Marie Curie Actions (MSCA)
- European Research Council (ERC) [339778] Funding Source: European Research Council (ERC)
- Swiss National Science Foundation (SNF) [P2EZP2_152216] Funding Source: Swiss National Science Foundation (SNF)
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.
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