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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 4. — Binding of Prp5 and binding of the tri-snRNP on the spliceosome are mutually exclusive. (A) Splicing reactions were carried out with wild-type, U257A, U257G, and U257C pre-mRNAs in Prp5-V5 extracts, and the reaction mixtures were precipitated with anti-Lea1, anti-V5, or anti-Prp8 antibody. (B) Spliceosomes assembled on wild-type, ACAC, U257A, U257G, and U257C biotinylated pre-mRNAs using Prp5-V5 extracts were pulled down with streptavidin-Sepharose, and the components were analyzed by Western blotting probed with anti-V5, anti-Lea1, anti-Prp8, and anti-Ntc20 antibodies. (C,D) Splicing reactions were carried out in Prp5-V5 extracts with wild-type, U257A, U257G, and U257 pre-mRNAs (C) The spliceosome was precipitated with anti-V5 antibody, and the components were analyzed by Northern blotting probed for five snRNAs. (D) The spliceosome was precipitated with anti-Lea1, anti-V5, or anti-Prp8 antibody, and the components were analyzed by Western blotting probed with anti-Snu114, anti-V5, and anti-Lea1 antibodies.