The SecA subunit of Escherichia coli preprotein translocase is exposed to the periplasm.
SecA undergoes conformational changes during translocation, inserting domains into and across the membrane or enhancing the protease resistance of these domains. We now show that some SecA bound at SecYEG is accessible from the periplasm to a membrane-impermeant probe in cells with a permeabilized outer membrane but an intact plasma membrane.
Eichler
J
J
Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755-3844, USA.
Wickner
W
W
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D001692:Biological Transport; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology*; D029968:Escherichia coli Proteins; D008239:Lysine / Q000031:analogs & derivatives / Q000494:pharmacology; D008301:Maleimides / Q000494:pharmacology; D008565:Membrane Proteins / Q000378:metabolism; D026901:Membrane Transport Proteins; D019897:Periplasm / Q000378:metabolism; D011498:Protein Precursors / Q000378:metabolism*; D000069816:SEC Translocation Channels; D000081416:SecA Proteins; D014357:Trypsin / Q000378:metabolism
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008301:Maleimides; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D011498:Protein Precursors; D000069816:SEC Translocation Channels; C065493:SecE protein, E coli; C088616:SecG protein, E coli; C057841:SecY protein, E coli; C047272:3-(N-maleimidopropionyl)biocytin; D014357:Trypsin; D000251:Adenosine Triphosphatases; D000081416:SecA Proteins; D008239:Lysine