Topologically fixed SecG is fully functional.
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.
van der Sluis
Eli O
EO
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.
van der Vries
Erhard
E
Berrelkamp
Greetje
G
Nouwen
Nico
N
Driessen
Arnold J M
AJ
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
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D000069816:SEC Translocation Channels; C088616:SecG protein, E coli