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. 2015 Jan 1;29(1):81–93. doi: 10.1101/gad.253708.114

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© 2015 Liang and Cheng; 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 5. — Prp5 mutants facilitate the association of tri-snRNP. (A) Splicing reactions were performed with wild-type, U257A, U257G, or U257C pre-mRNA in Prp5-depleted cus2∆ extracts without (lanes 1–4) or with the addition of wild-type Prp5 (lanes 5–8), prp5-N399D (lanes 9–12), or prp5-TAG (lanes 13–16) recombinant protein. The reaction mixtures were immunoprecipitated with anti-Lea1, anti-V5, or anti-Prp8 antibody. RNA was quantified by a PhosphorImager, and the molar ratios of total RNA precipitated by anti-V5 and anti-Prp8 antibodies to those precipitated by anti-Lea1 antibody are plotted in a bar graph. (B) The same as in A, with wild-type or U257G pre-mRNA for the splicing reaction using prp5-E235A (lanes 9–12) and prp5-AAAA (lanes 13–16) mutants. (C) Assays for the ATPase activity of wild-type and E235A and AAAA mutants of Prp5.