Chromosomal His-tagging: an alternative approach to membrane protein purification.
Membrane proteins are of keen interest to structural biologists, as they are known to act as receptors, adhesins, sensors, transporters, and signal-transducers of living cells. During the past few decades, the efforts made to study the bacterial membrane proteins have been impaired by the problems encountered during the production and purification of native proteins. Herein we demonstrate that the Campylobacter jejuni CadF protein, which was isolated using a novel purification strategy, exhibits biological activity as evidenced by channel activity in lipid bilayers. CadF, an E. coli OmpA-like protein, facilitates the binding of C. jejuni to the extracellular matrix component, fibronectin.
Mamelli
Laurent
L
UMR-MD1, IFR 48, Faculté de Médecine, Université de la Méditerranée, Marseille Cedex, France.
Dedieu
Luc
L
Dé
Emmanuelle
E
Konkel
Michael E
ME
Pagès
Jean-Marie
JM
Bolla
Jean-Michel
JM
D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000302:isolation & purification*; D016123:Campylobacter jejuni / Q000235:genetics / Q000378:metabolism; D002352:Carrier Proteins / Q000235:genetics / Q000302:isolation & purification*; D002876:Chromosomes, Bacterial / Q000378:metabolism*; D005822:Genetic Vectors; D006639:Histidine; D009842:Oligopeptides; D010957:Plasmids
D001425:Bacterial Outer Membrane Proteins; C107872:CadF protein, Campylobacter jejuni; D002352:Carrier Proteins; C471213:His-His-His-His-His-His; D009842:Oligopeptides; D006639:Histidine