6Y6E

drosophila Unr CSD456

Summary for 6Y6E

• Entry DOI: 10.2210/pdb6y6e/pdb
• Descriptor: Upstream of N-ras, isoform A, ETHYL MERCURY ION (3 entities in total)
• Functional Keywords: csd, nccsd, rna binding protein
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 30363.96

Authors

Hollmann, N.M.,Jagtap, P.K.A.,Hennig, J. (deposition date: 2020-02-26, release date: 2020-07-29, Last modification date: 2024-05-15)

Primary citation

Hollmann, N.M.,Jagtap, P.K.A.,Masiewicz, P.,Guitart, T.,Simon, B.,Provaznik, J.,Stein, F.,Haberkant, P.,Sweetapple, L.J.,Villacorta, L.,Mooijman, D.,Benes, V.,Savitski, M.M.,Gebauer, F.,Hennig, J.
Pseudo-RNA-Binding Domains Mediate RNA Structure Specificity in Upstream of N-Ras.
Cell Rep, 32:107930-107930, 2020

PubMed Abstract: 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.

PubMed: 32697992
DOI: 10.1016/j.celrep.2020.107930

Experimental method

X-RAY DIFFRACTION (2.02 Å)