The active protein-conducting channel of Escherichia coli contains an apolar patchBol, R., de Wit, J. G. & Driessen, A. J. M., 12-Oct-2007, In : The Journal of Biological Chemistry. 282, 41, p. 29785-29793 9 p.
Research output: Contribution to journal › Article › Academic › peer-review
Protein translocation across the cytoplasmic membrane of Escherichia coli is mediated by translocase, a complex of a protein conducting channel, SecYEG, and a peripheral motor domain, SecA. SecYEG has been proposed to constitute an aqueous path for proteins to pass the membrane in an unfolded state. To probe the solvation state of the active channel, the polarity sensitive fluorophore N-(( 2-( iodoacetoxy) ethyl)- N- methyl) amino- 7- nitrobenz- 2- oxa- 1,3- diazole was introduced at specific positions in the C- terminal region of the secretory protein proOmpA. Fluorescence measurements with defined proOmpA- DHFR translocation intermediates indicate mostly a water- exposed environment with a hydrophobic region in the center of the channel.
|Number of pages||9|
|Journal||The Journal of Biological Chemistry|
|Publication status||Published - 12-Oct-2007|
- ER MEMBRANE, TRANSLOCATION CHANNEL, PREPROTEIN TRANSLOCASE, PRECURSOR PROTEIN, PLASMA-MEMBRANE, CHAPERONE SECB, ENDOPLASMIC-RETICULUM, CYTOPLASMIC MEMBRANE, DISULFIDE BRIDGE, CATALYTIC CYCLE