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. 2011 May 15;22(10):1638–1647. doi: 10.1091/mbc.E10-12-0943

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© 2011 Müller 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 5: — The assembly of YadA-MA depends on Tim8/Tim13 and Mas37. (A and C) Mitochondria isolated from either tom20Δ (A) or tim8Δ/tim13Δ (C) and their corresponding wild-type strains transformed with either YadA-MA or PhoE were analyzed by SDS–PAGE and immunodecoration with antibodies against either HA-tag or PhoE, respectively. In addition, immunodecoration with antibodies against the indicated mitochondrial proteins was performed. (B and D) Mitochondria isolated from either tom70Δ/tom71Δ (B) or mas37Δ (D) and their corresponding wild-type cells transformed with YadA-MA were analyzed as in (A). (E) YadA-MA was transformed into cells expressing Tob55 under the control of the GAL10 promoter. Cells were harvested at the indicated time points after a shift from galactose- to glucose-containing medium. Crude mitochondria were isolated, and proteins were analyzed by SDS–PAGE and immunodecoration with antibodies against HA-tag and the indicated mitochondrial proteins. The monomeric and trimeric forms of YadA-MA are indicated with M and T, respectively. Tob55, Tom40, and porin are β-barrel proteins.