Neisserial Omp85 protein is selectively recognized and assembled into functional complexes in the outer membrane of human mitochondria.

ABSTRACT: As a consequence of their bacterial origin, mitochondria contain β-barrel proteins in their outer membrane (OMM). These proteins require the translocase of the outer membrane (TOM) complex and the conserved sorting and assembly machinery (SAM) complex for transport and integration into the OMM. The SAM complex and the β-barrel assembly machinery (BAM) required for biogenesis of β-barrel proteins in bacteria are evolutionarily related. Despite this homology, we show that bacterial β-barrel proteins are not universally recognized and integrated into the OMM of human mitochondria. Selectivity exists both at the level of the TOM and the SAM complex. Of all of the proteins we tested, human mitochondria imported only β-barrel proteins originating from Neisseria sp., and only Omp85, the central c

SUBMITTER: Kozjak-Pavlovic V 

PROVIDER: S-EPMC3143660 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature