Construction and in vivo analysis of new split lactose permeases

FEBS Letters

Wrubel, Wolfgang¹  Ehring, Ruth¹  Stochaj, Ursula² 

[1]Institut fuer Genetik der Universitaet zu Koeln, D-50931 Koeln, Germany

[2]McGill University, Montreal, Que. H3G 1 Y6, Canada

关键词: LacY permease;    Lactose transport;    Functional complementation;    Protein helix duplication;    CCCP;    carbonylcyanide m-chlorophenylhydrazone;    IPTG;    isopropyl-β-d-thiogalactopyranoside;    NEM;    N-ethylmaleimide;    TDG;    d-galactopyranosyl-β-d-thiogalactopyranoside;   

DOI  :  10.1016/0014-5793(94)00719-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The capacity of incomplete segments of Escherichia coli lactose permease to form transport-competent complexes in vivo was further tested. Two series of mutant lacY genes were constructed. One encoded N-terminal lactose permease segments of different length. The proteins specified by the other group contained deletions of different length and location within the N-terminal region. Several pairs of such mutant proteins reconstituted active lactose transport. For certain combinations duplications of protein segments were compatible with the formation of an active carrier. Duplication of helices could also be tolerated, when part of a single polypeptide chain.

【 授权许可】

Unknown