Scientific article

Deregulation of the SecYEG translocation channel upon removal of the plug domain

Published inThe Journal of biological chemistry, vol. 282, no. 2, p. 1281-1287
Publication date2007

Previous studies have shown that the SecY plug is displaced from the center of the SecYEG channel during polypeptide translocation. The structural and functional consequences of the deletion of the plug are now examined. Both in vivo and in vitro observations indicate that the plug domain is not essential to the function of the translocon. In fact, deletion of the plug confers to the cell and to the membranes a Prl-like phenotype: reduced proton-motive force dependence of translocation, increased membrane insertion of SecA, diminished requirement for functional leader peptide, and weakened SecYEG subunit association. Although the plug domain does not seem essential, locking the plug in the center of the channel inactivates the translocon. Thus, the SecY plug is important to regulate the activity of the channel and to confer specificity to the translocation reaction. We propose that the plug contributes to the gating mechanism of the channel by maintaining the structure of the SecYEG complex in a compact closed state.

  • Crystallography
  • Escherichia coli/ metabolism
  • Escherichia coli Proteins/ chemistry/ metabolism
  • Membrane Proteins/chemistry/metabolism
  • Multiprotein Complexes/ chemistry/ metabolism
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Protein Transport/physiology
Affiliation Not a UNIGE publication
Citation (ISO format)
MAILLARD, A. P. et al. Deregulation of the SecYEG translocation channel upon removal of the plug domain. In: The Journal of biological chemistry, 2007, vol. 282, n° 2, p. 1281–1287. doi: 10.1074/jbc.M610060200
Main files (1)
ISSN of the journal0021-9258

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