Journal
CELL REPORTS
Volume 32, Issue 3, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2020.107930
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Funding
- EIPOD fellowship
- Marie Curie Actions Cofund grant MSCA-COFUND-FP
- Spanish Ministry of Science and Innovation and Universities (MICINN) [PGC2018-099697-B-100]
- la Caixa'' Foundation [100010434, LCF/PR/HR17/52150016]
- Catalan Government [2017SGR534]
- Centre of Excellence Severo Ochoa
- Emmy-Noether Fellowship
- Deutsche Forschungsgemeinschaft (DFG) [SPP1935]
- EMBL
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RNA-binding proteins (RBPs) commonly feature multiple RNA-binding domains (RBDs), which provide these proteins with a modular architecture. Accumulating evidence supports that RBP architectural modularity and adaptability define the specificity of their interactions with RNA. However, how multiple RBDs recognize their cognate single-stranded RNA (ssRNA) sequences in concert remains poorly understood. Here, we use Upstream of N-Ras (Unr) as a model system to address this question. Although reported to contain five ssRNA-binding cold-shock domains (CSDs), we demonstrate that Unr includes an additional four CSDs that do not bind RNA (pseudo-RBDs) but are involved in mediating RNA tertiary structure specificity by reducing the conformational heterogeneity of Unr. Disrupting the interactions between canonical and non-canonical CSDs impacts RNA binding, Unr-mediated translation regulation, and the Unr-dependent RNA interactome. Taken together, our studies reveal a new paradigm in protein-RNA recognition, where interactions between RBDs and pseudo-RBDs select RNA tertiary structures, influence RNP assembly, and define target specificity.
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