Formation of disulfide bonded dimer of mutated heat‐labile enterotoxin in vivo

FEBS Letters

Hardy, Simon J.S.¹  Hedges, Peter A.¹ 

[1] Department of Biology, University of York, York YO1 5DD, UK

关键词: Heat-labile enterotoxin;    Disulfide bond;    Membrane association;    DTT;    dithiothreitol;    IPTG;    isopropylthiogalactoside;   

DOI  :  10.1016/0014-5793(96)00082-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

One of the two cysteines in the B subunit of heatlabile enterotoxin has been changed to a serine by site-directed mutagenesis so that the internal disulfide bond cannot form. The mutant protein, like the wild-type protein synthesised in the presence of the reducing agent dithiothreitol, does not form pentamers in the periplasm but binds to available membranes. Binding to membranes is disrupted by chaotropic agents but not by salt. More than half the molecules of mutant protein form disulfide-bonded dimers when exported to the periplasm but no dimer is detected when the protein is exported to the medium by spheroplasts.

【 授权许可】

Unknown