LUKAVSKY, Peter, Dalia DAUJOTYTE, James R TOLLERVEY, Jernej ULE, Cristiana STUANI, Emanuele BURATTI, Francisco E BARALLE, Fred F DAMBERGER and 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, 2013, vol. 20, No 12, p. 1443-1449. ISSN 1545-9993. Available from: https://dx.doi.org/10.1038/nsmb.2698. |
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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 and 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, 2013, vol.~20, No~12, p.~1443-1449. ISSN~1545-9993. Available from: https://dx.doi.org/10.1038/nsmb.2698.
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