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Assembly of eukaryotic class III (N‐out, C‐in) membrane proteins into the Escherichia coli cytoplasmic membrane
Author(s) -
Hennessey Emma S.,
Hashemzadeh-Bonehi Lily,
Hunt Lesley A.,
Broome-Smith Jenny K.
Publication year - 1993
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(93)80317-n
Subject(s) - glycophorin , spheroplast , cytoplasm , escherichia coli , membrane topology , membrane protein , signal peptide , biochemistry , bacterial outer membrane , biology , membrane , chemistry , microbiology and biotechnology , peptide sequence , gene
Class III membrane proteins lack cleavable signal peptides but adopt an N‐out, C‐in topology with respect to their native membranes. We have analysed the fate of two eukaryotic class III plasma membrane proteins, human erythrocyte glycophorin C and influenza A virus M2 protein, in Escherichia coli . The N‐terminal domains of both proteins were efficiently localised to the extracytoplasmic side of the bacterial cytoplasmic membrane. When β‐lactamase was fused to the C‐terminus of glycophorin C it was localised to the cytoplasm, and protease treatment of spheroplasts caused a reduction in size of the fusion protein consistent with glycophorin C adopting its native topology in E. coli .