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. 2009 Jun 15;185(6):1029–1045. doi: 10.1083/jcb.200812018

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© 2009 Tamura et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 6. — Analysis of protein–protein interactions in the TIM23 translocase in ups mutants. (A) Wild-type (WT) and ups1Δ mitochondria expressing Tim23p-Flag were solubilized in digitonin buffer containing the indicated concentrations of Triton X-100 and then incubated with anti-Flag agarose. 10% of lysate (Load) and 100% of bound proteins (Elute) were analyzed by immunoblotting. Band intensity was quantitated and normalized to samples not treated with Triton X-100. (B) Wild-type and mutant mitochondria expressing Tim23p-Flag were solubilized in digitonin buffer containing 0.025% Triton X-100 and subjected to coimmunoprecipitation (co-ip) with anti-Flag agarose. Band intensity was quantitated and normalized to that of wild-type mitochondria. (C) Coimmunoprecipitation was performed using mitochondria isolated from wild-type and pam17Δ cells expressing Tim23p-Flag and quantitated as described in A. (A–C) Values are mean ± SEM (n = 3).