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Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF

Author

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  • Cameron D. Mackereth

    (Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1
    Institut Européen de Chimie et Biologie and Université de Bordeaux, 2 rue Robert Escarpit
    Structural and Computational Biology, European Molecular Biology Laboratory, Meyerhofstrasse 1)

  • Tobias Madl

    (Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1
    Munich Center for Integrated Protein Science and Chair Biomolecular NMR, Technische Universität München, Lichtenbergstrasse 4)

  • Sophie Bonnal

    (Centre de Regulació Genòmica, Universitat Pompeu Fabra, Dr. Aiguader 88)

  • Bernd Simon

    (Structural and Computational Biology, European Molecular Biology Laboratory, Meyerhofstrasse 1)

  • Katia Zanier

    (Structural and Computational Biology, European Molecular Biology Laboratory, Meyerhofstrasse 1)

  • Alexander Gasch

    (Structural and Computational Biology, European Molecular Biology Laboratory, Meyerhofstrasse 1)

  • Vladimir Rybin

    (Structural and Computational Biology, European Molecular Biology Laboratory, Meyerhofstrasse 1)

  • Juan Valcárcel

    (Centre de Regulació Genòmica, Universitat Pompeu Fabra, Dr. Aiguader 88
    Institució Catalana de Recerca i Estudis Avançats, Dr. Aiguader 88)

  • Michael Sattler

    (Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1
    Structural and Computational Biology, European Molecular Biology Laboratory, Meyerhofstrasse 1
    Munich Center for Integrated Protein Science and Chair Biomolecular NMR, Technische Universität München, Lichtenbergstrasse 4)

Abstract

Selection by cooperation Different domains of a protein can interact dynamically to recognize a ligand, but the coordination of binding by multiple domains is not well understood. Michael Sattler and colleagues have investigated binding of a polypurine tract RNA by tandem RNA recognition motifs (RRMs) of a splicing factor. The domains exist in equilibrium between two distinct conformations, which shifts based on the affinity of the tract for the RRMs. This work highlights the role that cooperative multi-domain conformational selection can have when sequence specificity is not strict.

Suggested Citation

  • Cameron D. Mackereth & Tobias Madl & Sophie Bonnal & Bernd Simon & Katia Zanier & Alexander Gasch & Vladimir Rybin & Juan Valcárcel & Michael Sattler, 2011. "Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF," Nature, Nature, vol. 475(7356), pages 408-411, July.
    • Handle: RePEc:nat:nature:v:475:y:2011:i:7356:d:10.1038_nature10171
    DOI: 10.1038/nature10171
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    Cited by:

    1. Komal Soni & Pravin Kumar Ankush Jagtap & Santiago Martínez-Lumbreras & Sophie Bonnal & Arie Geerlof & Ralf Stehle & Bernd Simon & Juan Valcárcel & Michael Sattler, 2023. "Structural basis for specific RNA recognition by the alternative splicing factor RBM5," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Anna Knörlein & Chris P. Sarnowski & Tebbe Vries & Moritz Stoltz & Michael Götze & Ruedi Aebersold & Frédéric H.-T. Allain & Alexander Leitner & Jonathan Hall, 2022. "Nucleotide-amino acid π-stacking interactions initiate photo cross-linking in RNA-protein complexes," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    3. Hanlun Jiang & Fu Kit Sheong & Lizhe Zhu & Xin Gao & Julie Bernauer & Xuhui Huang, 2015. "Markov State Models Reveal a Two-Step Mechanism of miRNA Loading into the Human Argonaute Protein: Selective Binding followed by Structural Re-arrangement," PLOS Computational Biology, Public Library of Science, vol. 11(7), pages 1-21, July.

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