Functional reassembly of the Escherichia coli maltose transporter following purification of a MalF-MalG subassembly

J Bacteriol. 2005 Apr;187(8):2908-11. doi: 10.1128/JB.187.8.2908-2911.2005.

Abstract

Taking advantage of a chaperone-like function of MalK, a stable complex of MalF-MalG could be solubilized from the Escherichia coli membrane and purified in high yield in the absence of MalK. This MalF-MalG complex was competent for efficient reassembly of a functional MalFGK(2) maltose transporter complex both in detergent solution and in proteoliposomes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • ATP-Binding Cassette Transporters / metabolism*
  • Escherichia coli / chemistry
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / metabolism*
  • Maltose / metabolism
  • Monosaccharide Transport Proteins / metabolism*

Substances

  • ATP-Binding Cassette Transporters
  • Escherichia coli Proteins
  • MalF protein, E coli
  • MalG protein, E coli
  • MalK protein, E coli
  • Monosaccharide Transport Proteins
  • maltose transport system, E coli
  • Maltose