Topologically fixed SecG is fully functional

J Bacteriol. 2006 Feb;188(3):1188-90. doi: 10.1128/JB.188.3.1188-1190.2006.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Biological Transport / physiology
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / physiology*
  • Membrane Proteins / chemistry
  • Membrane Proteins / physiology*
  • Membrane Transport Proteins / chemistry
  • Membrane Transport Proteins / physiology
  • Protein Transport*
  • SEC Translocation Channels

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Membrane Proteins
  • Membrane Transport Proteins
  • SEC Translocation Channels
  • SecG protein, E coli