Detection and identification of stable oligomeric protein complexes in Escherichi coli inner membranes: a proteomics approach.
In this study we present a new technology to detect stable oligomeric protein complexes in membranes. The technology is based on the ability of small membrane-active alcohols to dissociate the highly stable homotetrameric potassium channel KcsA. It is shown via a proteomics approach, using diagonal electrophoresis and nano-flow liquid chromatography coupled to tandem mass spectrometry, that a large number of both integral and peripheral Escherichia coli inner membrane proteins are part of stable oligomeric complexes that can be dissociated by small alcohols. This study gives insight into the composition and stability of these complexes.
Spelbrink
Robin E J
RE
Department Biochemistry of Membranes, Institute of Biomembranes and Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. r.e.jspelbrink@chem.uu.nl
Kolkman
Annemieke
A
Slijper
Monique
M
Killian
J Antoinette
JA
de Kruijff
Ben
B
D001426:Bacterial Proteins; D002462:Cell Membrane / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000302:isolation & purification; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000737:chemistry* / Q000302:isolation & purification; D015221:Potassium Channels / Q000737:chemistry* / Q000302:isolation & purification; D024642:Potassium Channels, Voltage-Gated; D020543:Proteome
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C504448:KcsA protein, Streptomyces coelicolor; D046911:Macromolecular Substances; D008565:Membrane Proteins; D015221:Potassium Channels; D024642:Potassium Channels, Voltage-Gated; D020543:Proteome