Proline-rich Sequence Recognition: I. MARKING GYF AND WW DOMAIN ASSEMBLY SITES IN EARLY SPLICEOSOMAL COMPLEXES

Molecular & Cellular Proteomics(2009)

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摘要
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. Molecular & Cellular Proteomics 8: 2461-2473, 2009.
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spliceosomes,catalysis,fluorescence resonance energy transfer,magnetic resonance spectroscopy,binding sites,rna splicing,cell line,mass spectrometry
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