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. 2012 Nov 15;23(22):4335–4346. doi: 10.1091/mbc.E12-05-0420

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© 2012 Schreiner 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: — Effect of Yme1 on aggregation of DHFR fusion proteins. (A) Isolated mitochondria (5 and 15 μg) were analyzed by SDS–PAGE and immunodecoration with indicated antibodies. (B and C) Mitochondria were solubilized with Triton X-100–containing buffer, and soluble (S) and aggregate (P, pellet) fractions were separated by centrifugation. Samples were analyzed by SDS–PAGE followed by immunodecoration with the indicated antibodies.