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The RNA fold interactome of evolutionary conserved RNA structures in S. cerevisiae

Nuria Casas-Vila, Sergi Sayols, Lara Pérez-Martínez, Marion Scheibe and Falk Butter ()
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Nuria Casas-Vila: Institute of Molecular Biology
Sergi Sayols: Institute of Molecular Biology
Lara Pérez-Martínez: Institute of Molecular Biology
Marion Scheibe: Institute of Molecular Biology
Falk Butter: Institute of Molecular Biology

Nature Communications, 2020, vol. 11, issue 1, 1-12

Abstract: Abstract RNA-binding proteins play key roles in regulation of gene expression via recognition of structural features in RNA molecules. Here we apply a quantitative RNA pull-down approach to 186 evolutionary conserved RNA structures and report 162 interacting proteins. Unlike global RNA interactome capture, we associate individual RNA structures within messenger RNA with their interacting proteins. Of our binders 69% are known RNA-binding proteins, whereas some are previously unrelated to RNA binding and do not harbor canonical RNA-binding domains. While current knowledge about RNA-binding proteins relates to their functions at 5′ or 3′-UTRs, we report a significant number of them binding to RNA folds in the coding regions of mRNAs. Using an in vivo reporter screen and pulsed SILAC, we characterize a subset of mRNA-RBP pairs and thus connect structural RNA features to functionality. Ultimately, we here present a generic, scalable approach to interrogate the increasing number of RNA structural motifs.

Date: 2020
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DOI: 10.1038/s41467-020-16555-4

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