LOUGHLIN, F.E., Peter LUKAVSKY, T. KAZEEVA, S. REBER, E.M. HOCK, M. COLOMBO, C. VON SCHROETTER, P. PAULI, A. CLERY, O. MUHLEMANN, M. POLYMENIDOU, M.D. RUEPP a F.H.T. ALLAIN. The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity. Molecular Cell. CAMBRIDGE: CELL PRESS, 2019, roč. 73, č. 3, s. 490-510. ISSN 1097-2765. Dostupné z: https://dx.doi.org/10.1016/j.molcel.2018.11.012. |
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@article{1611558, author = {Loughlin, F.E. and Lukavsky, Peter and Kazeeva, T. and Reber, S. and Hock, E.M. and Colombo, M. and Von Schroetter, C. and Pauli, P. and Clery, A. and Muhlemann, O. and Polymenidou, M. and Ruepp, M.D. and Allain, F.H.T.}, article_location = {CAMBRIDGE}, article_number = {3}, doi = {http://dx.doi.org/10.1016/j.molcel.2018.11.012}, keywords = {NUCLEAR IMPORT RECEPTOR; PHASE-SEPARATION; CRYSTAL-STRUCTURE; BINDING PROTEINS; NMR STRUCTURE; ZINC FINGERS; ALS; DOMAIN; GRANULES; IDENTIFICATION}, language = {eng}, issn = {1097-2765}, journal = {Molecular Cell}, title = {The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity}, url = {https://www.sciencedirect.com/science/article/pii/S1097276518309821?via%3Dihub}, volume = {73}, year = {2019} }
TY - JOUR ID - 1611558 AU - Loughlin, F.E. - Lukavsky, Peter - Kazeeva, T. - Reber, S. - Hock, E.M. - Colombo, M. - Von Schroetter, C. - Pauli, P. - Clery, A. - Muhlemann, O. - Polymenidou, M. - Ruepp, M.D. - Allain, F.H.T. PY - 2019 TI - The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity JF - Molecular Cell VL - 73 IS - 3 SP - 490 EP - 490 PB - CELL PRESS SN - 10972765 KW - NUCLEAR IMPORT RECEPTOR KW - PHASE-SEPARATION KW - CRYSTAL-STRUCTURE KW - BINDING PROTEINS KW - NMR STRUCTURE KW - ZINC FINGERS KW - ALS KW - DOMAIN KW - GRANULES KW - IDENTIFICATION UR - https://www.sciencedirect.com/science/article/pii/S1097276518309821?via%3Dihub L2 - https://www.sciencedirect.com/science/article/pii/S1097276518309821?via%3Dihub N2 - Fused in sarcoma (FUS) is an RNA binding protein involved in regulating many aspects of RNA processing and linked to several neurodegenerative diseases. Transcriptomics studies indicate that FUS binds a large variety of RNA motifs, suggesting that FUS RNA binding might be quite complex. Here, wepresent solution structures ofFUSzincfinger (ZnF) and RNA recognition motif (RRM) domains bound to RNA. These structures show a bipartite binding mode of FUS comprising of sequence-specific recognition of a NGGU motif via the ZnF and an unusual shape recognition of a stem-loop RNA via the RRM. In addition, sequence-independent interactions via the RGG repeats significantly increase binding affinity and promote destabilization of structured RNA conformation, enabling additional binding. We further show that disruption of the RRM and ZnF domains abolishes FUS function in splicing. Altogether, our results rationalize why deciphering the RNA binding mode of FUS has been so challenging. ER -
LOUGHLIN, F.E., Peter LUKAVSKY, T. KAZEEVA, S. REBER, E.M. HOCK, M. COLOMBO, C. VON SCHROETTER, P. PAULI, A. CLERY, O. MUHLEMANN, M. POLYMENIDOU, M.D. RUEPP a F.H.T. ALLAIN. The Solution Structure of FUS Bound to RNA Reveals a Bipartite Mode of RNA Recognition with Both Sequence and Shape Specificity. \textit{Molecular Cell}. CAMBRIDGE: CELL PRESS, 2019, roč.~73, č.~3, s.~490-510. ISSN~1097-2765. Dostupné z: https://dx.doi.org/10.1016/j.molcel.2018.11.012.
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