| LUKAVSKY, Peter, Dalia DAUJOTYTE, James R TOLLERVEY, Jernej ULE, Cristiana STUANI, Emanuele BURATTI, Francisco E BARALLE, Fred F DAMBERGER a H-T Allain FRÉDÉRIC. Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43. NATURE STRUCTURAL & MOLECULAR BIOLOGY. New York: NATURE PUBLISHING GROUP, roč. 20, č. 12, s. 1443-1449. ISSN 1545-9993. doi:10.1038/nsmb.2698. 2013. |
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@article{1136046,
author = {Lukavsky, Peter and Daujotyte, Dalia and Tollervey, James R and Ule, Jernej and Stuani, Cristiana and Buratti, Emanuele and Baralle, Francisco E and Damberger, Fred F and Frédéric, HandT Allain},
article_location = {New York},
article_number = {12},
doi = {http://dx.doi.org/10.1038/nsmb.2698},
keywords = {TDP-43; RNA recognition; RRM; CFTR},
language = {eng},
issn = {1545-9993},
journal = {NATURE STRUCTURAL & MOLECULAR BIOLOGY},
title = {Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43},
url = {http://www.nature.com/nsmb/journal/v20/n12/pdf/nsmb.2698.pdf},
volume = {20},
year = {2013}
}
TY - JOUR
ID - 1136046
AU - Lukavsky, Peter - Daujotyte, Dalia - Tollervey, James R - Ule, Jernej - Stuani, Cristiana - Buratti, Emanuele - Baralle, Francisco E - Damberger, Fred F - Frédéric, H-T Allain
PY - 2013
TI - Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43
JF - NATURE STRUCTURAL & MOLECULAR BIOLOGY
VL - 20
IS - 12
SP - 1443-1449
EP - 1443-1449
PB - NATURE PUBLISHING GROUP
SN - 15459993
KW - TDP-43
KW - RNA recognition
KW - RRM
KW - CFTR
UR - http://www.nature.com/nsmb/journal/v20/n12/pdf/nsmb.2698.pdf
L2 - http://www.nature.com/nsmb/journal/v20/n12/pdf/nsmb.2698.pdf
N2 - TDP-43 encodes an alternative-splicing regulator with tandem RNA-recognition motifs (RRMs). The protein regulates cystic fibrosis transmembrane regulator ( CFTR ) exon 9 splicing through binding to long UG-rich RNA sequences and is found in cytoplasmic inclusions of several neurodegenerative diseases. We solved the solution structure of the TDP-43 RRMs in complex with UG-rich RNA. Ten nucleotides are bound by both RRMs, and six are recognized sequence specifically. Among these, a central G interacts with both RRMs and stabilizes a new tandem RRM arrangement. Mutations that eliminate recognition of this key nucleotide or crucial inter-RRM interactions disrupt RNA binding and TDP-43–dependent splicing regulation. In contrast, point mutations that affect base-specific recognition in either RRM have weaker effects. Our findings reveal not only how TDP-43 recognizes UG repeats but also how RNA binding–dependent inter-RRM interactions are crucial for TDP-43 function.
ER -
LUKAVSKY, Peter, Dalia DAUJOTYTE, James R TOLLERVEY, Jernej ULE, Cristiana STUANI, Emanuele BURATTI, Francisco E BARALLE, Fred F DAMBERGER a H-T Allain FRÉDÉRIC. Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43. \textit{NATURE STRUCTURAL \&{} MOLECULAR BIOLOGY}. New York: NATURE PUBLISHING GROUP, roč.~20, č.~12, s.~1443-1449. ISSN~1545-9993. doi:10.1038/nsmb.2698. 2013.
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