Biogenesis of MalF and the MalFGK(2) maltose transport complex in Escherichia coli requires YidC

J Biol Chem. 2008 Jun 27;283(26):17881-90. doi: 10.1074/jbc.M801481200. Epub 2008 May 2.


The polytopic inner membrane protein MalF is a constituent of the MalFGK(2) maltose transport complex in Escherichia coli. We have studied the biogenesis of MalF using a combination of in vivo and in vitro approaches. MalF is targeted via the SRP pathway to the Sec/YidC insertion site. Despite close proximity of nascent MalF to YidC during insertion, YidC is not required for the insertion of MalF into the membrane. However, YidC is required for the stability of MalF and the formation of the MalFGK(2) maltose transport complex. Our data indicate that YidC supports the folding of MalF into a stable conformation before it is incorporated into the maltose transport complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / metabolism
  • ATP-Binding Cassette Transporters / physiology*
  • Biological Transport
  • Cell Membrane / metabolism
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / metabolism
  • Escherichia coli Proteins / physiology*
  • Gene Expression Regulation, Bacterial*
  • Maltose / metabolism*
  • Membrane Transport Proteins / metabolism
  • Membrane Transport Proteins / physiology*
  • Models, Biological
  • Monosaccharide Transport Proteins / metabolism
  • Monosaccharide Transport Proteins / physiology*
  • Plasmids / metabolism
  • Protein Binding
  • Protein Conformation
  • Protein Folding


  • ATP-Binding Cassette Transporters
  • Escherichia coli Proteins
  • MalF protein, E coli
  • MalG protein, E coli
  • MalK protein, E coli
  • Membrane Transport Proteins
  • Monosaccharide Transport Proteins
  • YIDC protein, E coli
  • Maltose