ArticleMethods in molecular biology (Clifton, N.J.)2014
Isolation and accumulation of spliceosomal assembly intermediates.
Article in Methods in molecular biology (Clifton, N.J.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- U2 snRNA structure is influenced by SF3A and SF3B proteins but not by SF3B inhibitors.PloS one · 2021Article
- Genetics and biochemistry remain essential in the structural era of the spliceosome.Methods (San Diego, Calif.) · 2017Review
- Mechanisms and Regulation of Alternative Pre-mRNA Splicing.Annual review of biochemistry · 2015Review
- Utilizing functional cell-free extracts to dissect ribonucleoprotein complex biology at single-molecule resolution.Wiley interdisciplinary reviews. RNAReview
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2 authors.
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Abstract
Isolating spliceosomes at a specific assembly stage requires a means to stall or enrich for one of the intermediate splicing complexes. We describe strategies to arrest spliceosomes at different points of complex formation and provide a detailed protocol developed for isolating intact splicing complexes arrested between the first and second chemical steps of splicing. Briefly, spliceosomes are assembled on a radiolabeled in vitro-transcribed splicing substrate from components present in nuclear extract of HeLa cells. Spliceosome progression is arrested after the first step of splicing chemistry by mutating the pre-mRNA substrate at the 3' splice site. The substrate also contains binding sites for the MS2 protein, which serve as an affinity tag. Purification of arrested spliceosomes is carried out in two steps: (1) size exclusion chromatography and (2) affinity selection via a fusion of MS2 and maltose-binding protein (MBP). Complex assembly and purification are analyzed by denaturing polyacrylamide gel electrophoresis.
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