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Chromosomal His‐tagging: An alternative approach to membrane protein purification
Author(s) -
Mamelli Laurent,
Dedieu Luc,
Dé Emmanuelle,
Konkel Michael E.,
Pagès JeanMarie,
Bolla JeanMichel
Publication year - 2007
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200600371
Subject(s) - campylobacter jejuni , membrane protein , bacterial adhesin , biology , fibronectin , biochemistry , bacterial outer membrane , membrane , microbiology and biotechnology , extracellular matrix , bacteria , escherichia coli , gene , genetics
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.