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Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F13%3A00070459" target="_blank" >RIV/00216224:14740/13:00070459 - isvavai.cz</a>

  • Result on the web

    <a href="http://www.nature.com/nsmb/journal/v20/n12/pdf/nsmb.2698.pdf" target="_blank" >http://www.nature.com/nsmb/journal/v20/n12/pdf/nsmb.2698.pdf</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/nsmb.2698" target="_blank" >10.1038/nsmb.2698</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Molecular basis of UG-rich RNA recognition by the human splicing factor TDP-43

  • Original language description

    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 affectbase-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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2013

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    NATURE STRUCTURAL & MOLECULAR BIOLOGY

  • ISSN

    1545-9993

  • e-ISSN

  • Volume of the periodical

    20

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    7

  • Pages from-to

    1443-1449

  • UT code for WoS article

    000328007600017

  • EID of the result in the Scopus database