Stroud DA, et al. (2011) Biogenesis of mitochondrial ?-barrel proteins: the POTRA domain is involved in precursor release from the SAM complex. Mol Biol Cell 22(16):2823-33
Abstract: The mitochondrial outer membrane contains proteinaceous machineries for the translocation of precursor proteins. The sorting and assembly machinery (SAM) is required for the insertion of ?-barrel proteins into the outer membrane. Sam50 is the channel-forming core subunit of the SAM complex and belongs to the BamA/Sam50/Toc75 family of proteins that have been conserved from Gram-negative bacteria to mitochondria and chloroplasts. These proteins contain one or more N-terminal polypeptide transport-associated (POTRA) domains. POTRA domains can bind precursor proteins, however, different views exist on the role of POTRA domains in the biogenesis of ?-barrel proteins. It has been suggested that the single POTRA domain of mitochondrial Sam50 plays a receptor-like function at the SAM complex. We established a system to monitor the interaction of chemical amounts of ?-barrel precursor proteins with the SAM complex of wild-type and mutant yeast in organello. We report that the SAM complex lacking the POTRA domain of Sam50 efficiently binds ?-barrel precursors, but is impaired in the release of the precursors. These results indicate the POTRA domain of Sam50 is not essential for recognition of ?-barrel precursors but functions in a subsequent step to promote the release of precursor proteins from the SAM complex.
|Status: Published||Type: Journal Article||PubMed ID: 21680715|
Topics addressed in this paper
Number of different genes curated to this paper: 7
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|Protein Physical Properties|
|Protein Sequence Features|
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