Topological analysis of the amino‐terminal region of lactose permease using the Escherichia coli outer membrane protein, OmpA, as a marker

FEBS Letters

Eschbach, Marie-Luise¹  Schwarz, Heinz¹  MacIntyre, Sheila¹  Ehring, Ruth² 

[1] Max-Planck-Institut für Biologie, Correnstrasse 38, D-7400 Tübingen, FRG;Institut für Genetik der Universität zu Köln, D-5000 Köln 41, FRG

关键词: Lactose permease;    Topology;    Signal sequence;    Protein;    OmpA;    Membrane assembly;   

DOI  :  10.1016/0014-5793(89)81378-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

LacY-ompA fusions, encoding the N-terminal 50, 71 or 143 residues of lactose permease, were constructed. The observed orientation of the OmpA part of each hybrid protein with respect to the plasma membrane supports current models of the N-terminus of Lac permease. Hybrids possessing the entire mature OmpA were very stable; those with only a part thereof were much less stable. Due to their in vivo stability and accessibility to antibody it is proposed that such hybrids may represent potential models to investigate the assembly pathway of lactose permease.

【 授权许可】

Unknown