Abstract
AbstractRNA G-quadruplexes (RG4s) are four-stranded structures known to control mRNA translation of cancer relevant genes. RG4 formation is pervasive in vitro but not in cellulo, indicating the existence of poorly characterized molecular machinery that remodels RG4s and maintains them unfolded. Here, we performed a quantitative proteomic screen to identify cytosolic proteins that interact with a canonical RG4 in its folded and unfolded conformation. Our results identified hnRNP H/F as important components of the cytoplasmic machinery modulating the structural integrity of RG4s, revealed their function in RG4-mediated translation and uncovered the underlying molecular mechanism impacting the cellular stress response linked to the outcome of glioblastoma.
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Reference69 articles.
1. Wang, Z. L. et al. Comprehensive genomic characterization of RNA-binding proteins across human cancers. Cell Rep. 22, 286–298 (2018).
2. Pereira, B., Billaud, M. & Almeida, R. RNA-binding proteins in cancer: old players and new actors. Trends Cancer 3, 506–528 (2017).
3. Cammas, A. & Millevoi, S. RNA G-quadruplexes: emerging mechanisms in disease. Nucleic Acids Res. 45, 1584–1595 (2017).
4. Huppert, J. L., Bugaut, A., Kumari, S. & Balasubramanian, S. G-quadruplexes: the beginning and end of UTRs. Nucleic Acids Res. 36, 6260–6268 (2008).
5. von Hacht, A. et al. Identification and characterization of RNA guanine-quadruplex binding proteins. Nucleic Acids Res. 42, 6630–6644 (2014).
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