title: Deregulation of the SecYEG translocation channel upon removal of the plug domain.
abstract: 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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Life Sciences Institute, Faculty of Medicine, University of British Columbia, Vancouver, British Columbia V6T1Z3, Canada.
authors.forename: Antoine P
authors.initials: AP
authors.lastname: Maillard
authors.forename: Shifana
authors.initials: S
authors.lastname: Lalani
authors.forename: Filo
authors.initials: F
authors.lastname: Silva
authors.forename: Dominique
authors.initials: D
authors.lastname: Belin
authors.forename: Franck
authors.initials: F
authors.lastname: Duong
mesh_terms: D003461:Crystallography; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism*; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021381:Protein Transport / Q000502:physiology; D000069816:SEC Translocation Channels
chemical_list: D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D046912:Multiprotein Complexes; D000069816:SEC Translocation Channels; C065493:SecE protein, E coli; C088616:SecG protein, E coli; C057841:SecY protein, E coli