Changes in the periplasmic linker and in the expression level affect the activity of ToxR and λ‐ToxR fusion proteins in Escherichia coli

FEBS Letters

Brenner, Sydney¹  Jappelli, Roberto¹ 

[1] The Molecular Sciences Institute, 2168 Shattuck Avenue, Berkeley, CA 94704, USA

关键词: Lambda repressor;    ToxR;    β-Lactamase;    Alkaline phosphatase;    Dimerization;    aa;    amino acid(s);    Ap;    ampicillin;    BCIP;    5-bromo-4-chloro-3-indolyl phosphate;    Bgal;    β-galactosidase;    Bla;    β-lactamase;    Cm;    chloramphenicol;    HLPD;    highest lysing phage dilution;    Km;    kanamycin;    PhoA;    alkaline phosphatase;   

DOI  :  10.1016/S0014-5793(98)00125-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In order to assess the potentiality of Vibrio cholerae ToxR protein and of bacteriophage λ repressor as indicators of the dimerization of periplasmic proteins in Escherichia coli, we have constructed a series of plasmids encoding transmembrane fusion proteins. The amino-terminal part, containing the DNA binding domain of either ToxR or λ repressor, is located in the cytoplasm and acts as reporter for dimerization. As models of periplasmic proteins we have used alkaline phosphatase (a dimer) and β-lactamase (a monomer). Both the expression level and the distance between the transmembrane segment and the periplasmic protein substantially affect the activity of the reporter domains.

【 授权许可】

Unknown