Journal article
Alternative function for the mitochondrial SAM complex in biogenesis of α-helical TOM proteins
D Stojanovski, B Guiard, V Kozjak-Pavlovic, N Pfanner, C Meisinger
Journal of Cell Biology | ROCKEFELLER UNIV PRESS | Published : 2007
Abstract
The mitochondrial outer membrane contains two preprotein translocases: the general translocase of outer membrane (TOM) and the β-barrel-specific sorting and assembly machinery (SAM). TOM functions as the central entry gate for nuclear-encoded proteins. The channel-forming Tom40 is a β-barrel protein, whereas all Tom receptors and small Tom proteins are membrane anchored by a transmembrane α-helical segment in their N- or C-terminal portion. Synthesis of Tom precursors takes place in the cytosol, and their import occurs via pre-existing TOM complexes. The precursor of Tom40 is then transferred to SAM for membrane insertion and assembly. Unexpectedly, we find that the biogenesis of α-helical T..
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