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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 2: — YadA-MA is assembled into mitochondria in a native trimeric conformation. (A) Atomic structure model of YadA-MA monomer with an HA-tag at its N-terminal (right) and trimeric form built from three monomers (left). Each YadA-MA monomer is composed of four β-strands that participate in the β-barrel structure and a linker domain (shown here as a helical structure). (B) YadA-MA is located in mitochondria. Lysate of cells expressing YadA-MA and fractions corresponding to mitochondria, ER, and cytosol were analyzed by SDS–PAGE and immunodecoration with antibodies against HA-tag, the mitochondrial protein Tom70, a marker protein for the cytosol (Bmh1), and the ER protein Erv2. Mitochondria isolated from untransformed wild-type cells were coanalyzed as a control. (C) Monomerization assay of YadA. Mitochondria isolated from yeast cells expressing YadA-MA and envelopes of E. coli–expressing YadA-MA were boiled for 5 min in Laemmli buffer without urea (input) or in Laemmli buffer containing 8 M urea for the indicated time periods. The samples were analyzed by SDS–PAGE and immunodecoration with HA-antibody. Molecular mass markers and the monomeric and trimeric forms of YadA are indicated (left and right, respectively).