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Topological analysis of the amino‐terminal region of lactose permease using the Escherichia coli outer membrane protein, OmpA, as a marker
Author(s) -
MacIntyre Sheila,
Eschbach Marie-Luise,
Schwarz Heinz,
Ehring Ruth
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81378-x
Subject(s) - lactose permease , permease , escherichia coli , lactose , biochemistry , membrane transport protein , membrane , lac operon , chemistry , biology , membrane protein , topology (electrical circuits) , gene , mathematics , combinatorics
Lac Y‐ omp A 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.