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Molecular & Cellular Proteomics 8:2461-2473, 2009.
© 2009 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Proline-rich Sequence Recognition

I. MARKING GYF AND WW DOMAIN ASSEMBLY SITES IN EARLY SPLICEOSOMAL COMPLEXES^*,

Michael Kofler, Michael Schuemann, Christian Merz^¶, Daniela Kosslick, Andreas Schlundt, Astrid Tannert^||, Michael Schaefer^||, Reinhard Lührmann^¶, Eberhard Krause and Christian Freund^,**

From the Protein Engineering Group, Leibniz Institute for Molecular Pharmacology and Freie Universität Berlin , Robert-Rössle-Strasse 10, 13125 Berlin, Germany,
Mass Spectrometry Group, Leibniz Institute for Molecular Pharmacology, Robert-Rössle-Strasse 10, 13125 Berlin, Germany,
¶Department of Cellular Biochemistry, Max Planck Institute of Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany, and
||Pharmacology Institute, Charité-Universitätsmedizin Berlin, Campus Benjamin Franklin, Thielallee 67-73, 14195 Berlin, Germany

Proline-rich sequences (PRS) and their recognition domains have emerged as transposable protein interaction modules during eukaryotic evolution. They are especially abundant in proteins associated with pre-mRNA splicing and likely assist in the formation of the spliceosome by binding to GYF and WW domains. Here we profile PRS-mediated interactions of the CD2BP2/52K GYF domain by a site-specific peptide inhibitor and stable isotope labeling/mass spectrometry analysis. Several PRS hubs with multiple proline-rich motifs exist that can recruit GYF and/or WW domains. Saturating the PRS sites by an isolated GYF domain inhibited splicing at the level of A complex formation. The interactions mediated by PRS are therefore important to the early phases of spliceosomal assembly.

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