Sec-translocase mediated membrane protein biogenesis.
Alpha-helical transmembrane proteins in bacteria are localized within the plasma membrane. The membrane assembly of these proteins requires protein devices for insertion into the lipid bilayer. In E. coli, membrane proteins require the SRP pathway components Ffh, 4.5S RNA and FtsY for membrane targeting and the SecYEGDF translocase and, in some cases, SecA, for translocation of hydrophilic domains. In addition, YidC, a recently discovered membrane protein, mediates the membrane integration and folding of hydrophobic domains of membrane proteins. In this review, we will describe the current status of the protein targeting and membrane integration pathways.
Dalbey
Ross E
RE
Department of Chemistry, The Ohio State University, 120 W. 18th Avenue, Columbus, OH 43210-1106, USA. dalbey@chemistry.ohio-state.edu <dalbey@chemistry.ohio-state.edu>
Chen
Minyong
M
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D002462:Cell Membrane / Q000502:physiology; D006090:Gram-Negative Bacteria / Q000502:physiology; D008565:Membrane Proteins / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000378:metabolism*; D017510:Protein Folding; D021381:Protein Transport / Q000502:physiology; D000069816:SEC Translocation Channels; D000081416:SecA Proteins
D001426:Bacterial Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D000069816:SEC Translocation Channels; D000251:Adenosine Triphosphatases; D000081416:SecA Proteins