Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68
| العنوان: | Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68 |
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| المؤلفون: | Oksana Gonchar, Marina Danilenko, Sushma Nagaraja Grellscheid, David J. Elliott, Ralf Stehle, Michael Sattler, Albert Lahat, N. Helge Meyer, Yilei Liu, Cyril Dominguez, Jaelle N. Foot, Hyun-Seo Kang, Ian C. Eperon, Caroline Dalgliesh, Mikael Feracci |
| المصدر: | Nat. Commun. 7:10355 (2016) Nature Communications Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016) Nature communications, 2016, Vol.7, pp.10355 [Peer Reviewed Journal] |
| بيانات النشر: | Nature Publishing Group, 2016. |
| سنة النشر: | 2016 |
| مصطلحات موضوعية: | Male, 0301 basic medicine, endocrine system, Science, Molecular Sequence Data, Exonic splicing enhancer, General Physics and Astronomy, RNA-binding protein, Biology, DNA-binding protein, Article, General Biochemistry, Genetics and Molecular Biology, Mice, Structure-Activity Relationship, 03 medical and health sciences, SR protein, Animals, Humans, Amino Acid Sequence, Nucleotide Motifs, Adaptor Proteins, Signal Transducing, Regulation of gene expression, Genetics, Multidisciplinary, urogenital system, Alternative splicing, RNA-Binding Proteins, RNA, General Chemistry, Protein Structure, Tertiary, Cell biology, DNA-Binding Proteins, Alternative Splicing, HEK293 Cells, 030104 developmental biology, RNA splicing, Dimerization |
| الوصف: | Sam68 and T-STAR are members of the STAR family of proteins that directly link signal transduction with post-transcriptional gene regulation. Sam68 controls the alternative splicing of many oncogenic proteins. T-STAR is a tissue-specific paralogue that regulates the alternative splicing of neuronal pre-mRNAs. STAR proteins differ from most splicing factors, in that they contain a single RNA-binding domain. Their specificity of RNA recognition is thought to arise from their property to homodimerize, but how dimerization influences their function remains unknown. Here, we establish at atomic resolution how T-STAR and Sam68 bind to RNA, revealing an unexpected mode of dimerization different from other members of the STAR family. We further demonstrate that this unique dimerization interface is crucial for their biological activity in splicing regulation, and suggest that the increased RNA affinity through dimer formation is a crucial parameter enabling these proteins to select their functional targets within the transcriptome. Sam68 and T-STAR are members of the STAR family of proteins, which regulate various aspects of RNA metabolism. Here, the authors reveal structural features required for alternative splicing regulation by these proteins. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccbc7cf6b97fcb4f1450fcb62967c9df https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=47783 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....ccbc7cf6b97fcb4f1450fcb62967c9df |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |