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Research Article

A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli.

J P Sarsero, P J Wookey, P Gollnick, C Yanofsky, A J Pittard
J P Sarsero
Department of Microbiology, University of Melbourne, Parkville, Victoria, Australia.
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P J Wookey
Department of Microbiology, University of Melbourne, Parkville, Victoria, Australia.
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P Gollnick
Department of Microbiology, University of Melbourne, Parkville, Victoria, Australia.
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C Yanofsky
Department of Microbiology, University of Melbourne, Parkville, Victoria, Australia.
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A J Pittard
Department of Microbiology, University of Melbourne, Parkville, Victoria, Australia.
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DOI: 10.1128/jb.173.10.3231-3234.1991
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ABSTRACT

The nucleotide sequence of tnaB of the tryptophanase operon of Escherichia coli is presented. TnaB is a tryptophan-specific permease that is homologous to Mtr, a second tryptophan-specific permease, and to TyrP, a tyrosine-specific permease. Each member of this family appears to contain 11 membrane-spanning domains.

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A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli.
J P Sarsero, P J Wookey, P Gollnick, C Yanofsky, A J Pittard
Journal of Bacteriology May 1991, 173 (10) 3231-3234; DOI: 10.1128/jb.173.10.3231-3234.1991

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A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli.
J P Sarsero, P J Wookey, P Gollnick, C Yanofsky, A J Pittard
Journal of Bacteriology May 1991, 173 (10) 3231-3234; DOI: 10.1128/jb.173.10.3231-3234.1991
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