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J. Biol. Chem., Vol. 264, Issue 20, 11663-11670, 07, 1989
B Eckert and CF Beck
The transposon Tn10-encoded tetracycline resistance protein TetA is an
integral membrane protein responsible for the export of tetracycline from
the cytoplasmic to the periplasmic side of the inner membrane of
Gram-negative bacteria. From a plot of the average hydrophobicity along the
sequence of this protein, a two-dimensional membrane topology with 12
transmembrane domains may be predicted. Using plasmid-bearing Escherichia
coli maxicells we specifically radiolabeled the TetA protein. The amino
terminus of this membrane protein was shown not to be processed, and its
location on the inner side of the cytoplasmic membrane was demonstrated by
a newly developed use of a chemical method. Spheroplasts and inside-out
vesicles of the TetA protein synthesizing maxicells were subjected to
limited digestion by proteases of different specificities. The TetA protein
was not accessible to proteases from the periplasmic side. On the inner
side of the cytoplasmic membrane, the carboxyl terminus and four sites
accessible to endoproteases could be identified. The cleavage sites are
proposed to be localized between amino acid residues 60-70, 110-130,
180-200, and at amino acid 327. These results allow the definition of a
model for the two-dimensional topology of the TetA protein.
Topology of the transposon Tn10-encoded tetracycline resistance protein within the inner membrane of Escherichia coli
Institut fur Biologie III, Albert-Ludwigs-Universitat Freiburg, West Germany.
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