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. 2017 May 1;28(9):1165–1176. doi: 10.1091/mbc.E16-10-0746

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© 2017 Defenouillère et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 4: — Tom1 interacts significantly with the light-sedimenting RQC complex. (A) Silver-staining analysis of the proteins fractionated from Rqc1-TAP (right) vs. negative control (left) purifications upon Cdc48 depletion. (B) Proteins associated with Rqc1-TAP complexes cosedimenting with fractions 4 and 5 (left) or the 60S (right) were identified by LC-MS/MS, and t tests of LFQ intensities for each protein were performed in comparison with the negative control. Statistical results are given in the form of volcano plots. The x-axis shows the log₂ of LFQ ratios between the samples, and the y-axis shows the –log₁₀ of the p value of each protein enrichment among statistical groups. The semicircular curve defines candidates that are significantly enriched according to a statistical t test. These purifications coupled with gradient fractionation were repeated four times. The list of proteins identified is given in Supplemental Dataset S1.