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• W2023759124 abstract "The Sec translocon of Escherichia coli mediates the export of numerous secretory and membrane proteins. To dissect the passage of an exported protein across the Sec translocon into consecutive steps, we generated in vitro translocation intermediates of a polypeptide chain, which by its N-terminus is anchored in the membrane and by its C-terminus tethered to the ribosome. We find that in this situation, the motor protein SecA propagates translocation of a peptide loop across SecYEG prior to the removal of ribosomes. Upon SecA-driven exit from the translocon, this loop is brought into the immediate vicinity of the membrane-anchored, periplasmic chaperone PpiD. Consistent with a coupling between translocation across the SecYEG translocon and folding by periplasmic chaperones, a lack of PpiD retards the release of a translocating outer membrane protein into the periplasm." @default.
• W2023759124 created "2016-06-24" @default.
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• W2023759124 date "2008-04-26" @default.
• W2023759124 modified "2023-10-03" @default.
• W2023759124 title "The Periplasmic Chaperone PpiD Interacts with Secretory Proteins Exiting from the SecYEG Translocon" @default.
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• W2023759124 doi "https://doi.org/10.1021/bi800233w" @default.
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