Small Nuclear Ribonucleoprotein Remodeling During Catalytic Activation of the Spliceosome
Copyright policy )Small Nuclear Ribonucleoprotein Remodeling During Catalytic Activation of the Spliceosome
Major structural changes occur in the spliceosome during its activation just before catalyzing the splicing of pre–messenger RNAs (pre-mRNAs). Whereas changes in small nuclear RNA (snRNA) conformation are well documented, little is known about remodeling of small nuclear ribonucleoprotein (snRNP) structures during spliceosome activation. Here, human 45 S activated spliceosomes and a previously unknown 35 S U5 snRNP were isolated by immunoaffinity selection and were characterized by mass spectrometry. Comparison of their protein components with those of other snRNP and spliceosomal complexes revealed a major change in protein composition during spliceosome activation. Our data also suggest that the U5 snRNP is dramatically remodeled at this stage, with the Prp19 complex and other factors tightly associating, possibly in exchange for other U5 proteins, and suggest that after catalysis the remodeled U5 is eventually released from the postsplicing complex as a 35 S snRNP particle.
- University of Leicester United Kingdom
- Max Planck Society Germany
- Max Planck Institute for Multidisciplinary Sciences Germany
- European Molecular Biology Laboratory Germany
Models, Genetic, Macromolecular Substances, RNA Splicing, Nuclear Receptor Coactivators, Nuclear Proteins, Precipitin Tests, Catalysis, Mass Spectrometry, RNA, Small Nuclear, Centrifugation, Density Gradient, RNA Precursors, Spliceosomes, Humans, Ribonucleoprotein, U5 Small Nuclear, Transcription Factors
Models, Genetic, Macromolecular Substances, RNA Splicing, Nuclear Receptor Coactivators, Nuclear Proteins, Precipitin Tests, Catalysis, Mass Spectrometry, RNA, Small Nuclear, Centrifugation, Density Gradient, RNA Precursors, Spliceosomes, Humans, Ribonucleoprotein, U5 Small Nuclear, Transcription Factors
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