Folding outer membrane proteins independently of the β-barrel assembly machinery: an assembly pathway for multimeric complexes?
Since the discovery of the essential role of the β-barrel assembly machinery (BAM) for the membrane insertion of outer membrane proteins (OMPs) that are unrelated in sequence, members of this universally conserved family dominate discussions on OMP assembly in bacteria, mitochondria and chloroplasts. However, several multimeric bacterial OMPs assemble independently of the catalyzing BAM-component BamA. Recent progress on this alternative pathway is reviewed here, and a model for BAM-independent assembly for multimeric OMPs is proposed in which monomer delivery to the membrane and stable prepore formation are key steps towards productive membrane insertion.
Department of Physiology and Biophysics, Weill Cornell Medicine, New York, NY 10065, U.S.A. ghh2001@med.cornell.edu.
Gerard H M
GH
Huysmans
D001419:Bacteria / Q000378:metabolism*; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D002736:Chloroplasts / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D017510:Protein Folding; D055503:Protein Multimerization
D001425:Bacterial Outer Membrane Proteins
membrane protein folding; multimeric complex; outer membrane protein; secretin; β-barrel assembly machinery