Pseudo-RNA-Binding Domains Mediate RNA Structure Specificity in Upstream of N-Ras
| العنوان: | Pseudo-RNA-Binding Domains Mediate RNA Structure Specificity in Upstream of N-Ras |
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| المؤلفون: | Vladimir Benes, Nele Merret Hollmann, Mikhail M. Savitski, Frank Stein, Bernd Simon, Pawel Masiewicz, Pravin Kumar Ankush Jagtap, Fátima Gebauer, Laura Villacorta, Janosch Hennig, Jan Provaznik, Lara Jayne Sweetapple, Per Haberkant, Tanit Guitart, Dylan Mooijman |
| المصدر: | Cell reports 32(3), 107930 (1-15) (2020). doi:10.1016/j.celrep.2020.107930 Cell Reports |
| بيانات النشر: | Elsevier BV, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | 0301 basic medicine, RNA-binding domains, RNA-binding proteins, Model system, RNA-binding protein, Computational biology, translation regulation, Biology, Interactome, Article, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, NMR spectroscopy, 0302 clinical medicine, Protein Domains, Translational regulation, ribonucleoproteins, Animals, Drosophila Proteins, Amino Acid Sequence, ddc:610, Nucleic acid structure, integrative structural biology, Ribonucleoprotein, Nucleic acid tertiary structure, RNA, DNA-Binding Proteins, Drosophila melanogaster, 030104 developmental biology, Protein Biosynthesis, cold-shock domains, Nucleic Acid Conformation, 030217 neurology & neurosurgery |
| الوصف: | Summary 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. Graphical Abstract Highlights • Discovery of non-canonical cold-shock domains • Non-canonical cold-shock domains do not bind RNA independently • Interdomain contacts mediate RNA structure specificity and impact translation • Determination of an Unr-dependent ribonucleoprotein (RNP) interactome Hollmann et al. show how non-RNA-binding domains within Drosophila Unr, an RNA-binding protein, contribute to its RNA target specificity. The selectivity is mediated by interdomain contacts to the RNA-binding cold-shock domains, which restrict the protein shape. |
| وصف الملف: | application/pdf |
| تدمد: | 2211-1247 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc37ce1e6065d05f064d57cadc6d3babTest https://doi.org/10.1016/j.celrep.2020.107930Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....dc37ce1e6065d05f064d57cadc6d3bab |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 22111247 |
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