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

Cameron D. Mackereth, Tobias Madl, Sophie Bonnal, Bernd Simon, Katia Zanier, Alexander Gasch, Vladimir Rybin, Juan Valcárcel and Michael Sattler ()
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Cameron D. Mackereth: Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1
Tobias Madl: Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1
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
Michael Sattler: Institute of Structural Biology, Helmholtz Zentrum München, Ingolstädter Landstrasse 1

Nature, 2011, vol. 475, issue 7356, 408-411

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.

Date: 2011
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DOI: 10.1038/nature10171

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