| Literature DB >> 25596888 |
Thomas Ulrich1, Doron Rapaport2.
Abstract
The vast majority of outer membrane (OM) proteins in Gram-negative bacteria belongs to the class of membrane-embedded β-barrel proteins. Besides Gram-negative bacteria, the presence of β-barrel proteins is restricted to the OM of the eukaryotic organelles mitochondria and chloroplasts that were derived from prokaryotic ancestors. The assembly of these proteins into the corresponding OM is in each case facilitated by a dedicated protein complex that contains a highly conserved central β-barrel protein termed BamA/YaeT/Omp85 in Gram-negative bacteria and Tob55/Sam50 in mitochondria. However, little is known about the exact mechanism by which these complexes mediate the integration of β-barrel precursors into the lipid bilayer. Interestingly, previous studies showed that during evolution, these complexes retained the ability to functionally assemble β-barrel proteins from different origins. In this review we summarize the current knowledge on the biogenesis pathway of β-barrel proteins in Gram-negative bacteria, mitochondria and chloroplasts and focus on the commonalities and divergences that evolved between the different β-barrel assembly machineries.Entities:
Keywords: BAM complex; BamA; Periplasmic chaperones; TOB complex; Tob55; β-Barrel proteins
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Year: 2014 PMID: 25596888 DOI: 10.1016/j.ijmm.2014.12.009
Source DB: PubMed Journal: Int J Med Microbiol ISSN: 1438-4221 Impact factor: 3.473