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. 2017 Dec 1;31(23-24):2416–2429. doi: 10.1101/gad.308163.117

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© 2018 Bao et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 4. — Affinity-purified ΔRES spliceosomes are partially disassembled upon addition of Prp2, Spp2, and ATP. Spliceosomal complexes formed in extracts from prp2-1 Δsnu17 yeast cells after initial heat inactivation of Prp2 (designated ΔRES B/B^act-like complexes) were affinity-purified, and 45S complexes were subjected to a second glycerol gradient after incubation with buffer (A), 2 mM ATP (B), or ATP, Prp2, and Spp2 (C). RNA was isolated from each gradient fraction, separated by denaturing PAGE, and detected by Northern blotting with ³²P-labeled probes against the snRNAs indicated at the right. The ³²P-labeled Actin pre-mRNA was detected by autoradiography. The percentage of the pre-mRNA or the indicated snRNAs in the boxed or underlined fractions is shown below the gel in B and C. (D) RNA was isolated from ΔRES B/B^act-like complexes and analyzed by native PAGE. Free U4 snRNA or U4 base-paired with U6 was subsequently visualized by Northern blotting with a ³²P probe complementary to U4 snRNA. The percentage of free U4 versus U4 base-paired with U6 was quantitated with a PhosphorImager and is shown below each lane.