Are bacterial 'autotransporters' really transporters?
Autotransporters are bacterial outer membrane proteins that consist of a large N-terminal extracellular domain ('passenger domain') and a C-terminal beta-barrel domain ('beta domain'). The beta domain was originally proposed to function as a channel that transports its own passenger domain across the outer membrane. Results of recent structural, biochemical and molecular genetic studies, however, have challenged this idea. Here I describe an alternative model in which translocation of the passenger domain is mediated by an exogenous factor (possibly a newly identified factor necessary for assembly of outer membrane proteins called 'Omp85/YaeT'), whereas the beta domain only targets the protein to the outer membrane and serves as a membrane anchor.
Bernstein
Harris D
HD
Genetics and Biochemistry Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Building 5, Room 201, 5 Memorial Drive, Bethesda, MD 20892-0538, USA. harris_bernstein@nih.gov
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D021381:Protein Transport
D001425:Bacterial Outer Membrane Proteins