| 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 and 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, vol. 73, No 3, p. 490-510. ISSN 1097-2765. Available from: https://dx.doi.org/10.1016/j.molcel.2018.11.012. |
Other formats:
BibTeX
LaTeX
RIS
@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 and 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, vol.~73, No~3, p.~490-510. ISSN~1097-2765. Available from: https://dx.doi.org/10.1016/j.molcel.2018.11.012.
|
