Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC

EMBO Rep. 2001 Jun;2(6):524-9. doi: 10.1093/embo-reports/kve108.

Abstract

Recent studies identified YidC as a novel membrane factor that may play a key role in membrane insertion of inner membrane proteins (IMPs), both in conjunction with the Sec-translocase and as a separate entity. Here, we show that the type II IMP FtsQ requires both the translocase and, to a lesser extent, YidC in vivo. Using photo-crosslinking we demonstrate that the transmembrane (TM) domain of the nascent IMP FtsQ inserts into the membrane close to SecY and lipids, and moves to a combined YidC/lipid environment upon elongation. These data are consistent with a crucial role for YidC in the lateral transfer of TM domains from the Sec translocase into the lipid bilayer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Bacterial Proteins / metabolism*
  • Carrier Proteins / metabolism*
  • Cell Membrane / enzymology*
  • Cell Membrane / metabolism
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / enzymology
  • Escherichia coli / metabolism
  • Escherichia coli Proteins*
  • Lipid Metabolism
  • Membrane Proteins / metabolism*
  • Membrane Transport Proteins*
  • Models, Biological
  • Plasmids / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • RNA, Messenger / metabolism
  • Ribosomes / metabolism
  • SEC Translocation Channels
  • SecA Proteins

Substances

  • Bacterial Proteins
  • Carrier Proteins
  • Escherichia coli Proteins
  • FtsQ protein, E coli
  • Membrane Proteins
  • Membrane Transport Proteins
  • RNA, Messenger
  • SEC Translocation Channels
  • SecY protein, E coli
  • YIDC protein, E coli
  • Adenosine Triphosphatases
  • SecA Proteins