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. 2017 Mar;23(3):406–419. doi: 10.1261/rna.059667.116

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© 2017 Han et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 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 6. — Trm140 interacts with Ses1. (A) SDS-PAGE analysis reveals three polypeptide bands that copurify with Trm140. Strains containing either P_GAL-ORF240-PT or P_GAL-GLN4-MORF were grown as described in Materials and Methods, ORF240 and Gln4 were affinity purified under conditions identical to those used for pull-down assays, and proteins were analyzed by SDS-PAGE and Coomassie staining. Three distinct copurifying bands that were found in the ORF240 preparation (lane 3) are labeled A–C. (B) Chromosomally expressed Ses1-Myc and Trm140-cMORF interact. Trm140 was affinity purified from crude extracts of the indicated strains, using IgG Sepharose and 3C protease cleavage. Crude extract (input) was subjected to immunoblot analysis with anti-HA and anti-(c-myc) antibody, and IgG-purified protein (immunoprecipitate, IP) was analyzed by immunoblot with anti-(c-myc) antibody. (C) Overproduction of ORF240-PT results in increased copurification of Ses1. Trm140 was purified from a chromosomally tagged Trm140-cMORF strain, ORF240 was purified from a strain overexpressing ORF240-PT, and the amount of copurifying Ses1 was compared by immunoblot, as described in B.