title: Topologically fixed SecG is fully functional.
abstract: It has been proposed that the bitopic membrane protein SecG undergoes topology inversion during translocation of (pre)proteins via SecYEG. Here we show that SecG covalently cross-linked to SecY cannot invert its topology while remaining fully functional in protein translocation. Our results strongly disfavor topology inversion of SecG during protein translocation.
authors.affiliation: Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and Materials Science Center Plus, Kerklaan 30, University of Groningen, 9751 NN Haren, The Netherlands.
authors.forename: Eli O
authors.initials: EO
authors.lastname: van der Sluis
authors.forename: Erhard
authors.initials: E
authors.lastname: van der Vries
authors.forename: Greetje
authors.initials: G
authors.lastname: Berrelkamp
authors.forename: Nico
authors.initials: N
authors.lastname: Nouwen
authors.forename: Arnold J M
authors.initials: AJ
authors.lastname: Driessen
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001692:Biological Transport / Q000502:physiology; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000502:physiology*; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology*; D026901:Membrane Transport Proteins / Q000737:chemistry / Q000502:physiology; D021381:Protein Transport; D000069816:SEC Translocation Channels
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D000069816:SEC Translocation Channels; C088616:SecG protein, E coli