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Proline-rich sequence recognition: I. Marking GYF and WW domain assembly sites in early spliceosomal complexes.

ABSTRACT: 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.

SUBMITTER: Kofler M

PROVIDER: S-EPMC2773714 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature

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Proline-rich sequence recognition: I. Marking GYF and WW domain assembly sites in early spliceosomal complexes.

Kofler Michael M Schuemann Michael M Merz Christian C Kosslick Daniela D Schlundt Andreas A Tannert Astrid A Schaefer Michael M Lührmann Reinhard R Krause Eberhard E Freund Christian C

Molecular & cellular proteomics : MCP 20090530 11

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 multip ...[more]

PMID: 19483244

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