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. 2014 Sep;20(9):1465–1475. doi: 10.1261/rna.045252.114

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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 7. — Inability of Pat1C to interact with the Lsm1-7 complex is not due to phosphorylation. (A) Lsm1-7 complex was pulled down using Ni-NTA matrix from the lysates of pat1Δ cells that express Pat1C, Flag-Pat1C, or Flag-Pat1C-AA (indicated on top) from a CEN plasmid followed by Western analysis using anti-Flag antibodies of the lysate and pull-down samples. Two independent transformants expressing Flag-Pat1C-AA were used for the experiment. (B) pat1Δ cells expressing Pat1C were grown in glucose containing medium to log phase and then transferred to fresh medium that contains or lacks glucose for 30 min before they were pelleted and lysed. The Lsm1-7 complex was pulled down from the lysates using Ni-NTA matrix followed by Western analysis using anti-Flag antibodies of the lysate and pull-down samples. (C) Lsm1-7 complex purified from pat1Δ yeast was incubated with Pat1C or Pat1C-EE purified from E. coli or BSA and then bound to the anti-Flag antibody matrix. After washing to remove unbound proteins, the bound proteins were eluted, separated by SDS-PAGE, and visualized by silver staining (left panel). (Right) Silver-stained SDS-PAGE of purified Pat1C and Pat1C-EE.