Following the leader: bacterial protein export through the Sec pathway.
Significant strides have been made during the past 20 years in our understanding of protein secretion across the bacterial inner membrane. Specialized chaperones select secretory polypeptide chains and usher them to a membrane-embedded preprotein translocase. This unique molecular machine envelops the polymeric substrate and migrates along its length in defined, energy-dependent steps. Consequently, preproteins are gradually pumped into the periplasm where they acquire their native, folded conformation.
Economou
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Institute of Molecular Biology and Biotechnology-FORTH, Iraklio, Crete, GR-71110, Greece. aeconomo@imbb.forth.gr
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D001419:Bacteria / Q000254:growth & development / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D017510:Protein Folding; D011498:Protein Precursors / Q000378:metabolism; D000069816:SEC Translocation Channels; D000081416:SecA Proteins
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D026901:Membrane Transport Proteins; D011498:Protein Precursors; D000069816:SEC Translocation Channels; D000251:Adenosine Triphosphatases; D000081416:SecA Proteins