A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli
Open Access
- 1 May 1991
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 173 (10) , 3231-3234
- https://doi.org/10.1128/jb.173.10.3231-3234.1991
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.Keywords
This publication has 26 references indexed in Scilit:
- A consensus structure for membrane transportResearch in Microbiology, 1990
- Observations concerning topology and locations of helix ends of membrane proteins of known structureThe Journal of Membrane Biology, 1990
- β-GALACTOSIDE TRANSPORT IN E. COLI: A FUNCTIONAL DISSECTION OF LAC PERMEASEPublished by Elsevier ,1990
- The transmembrane topology of the sn‐glycerol‐3‐phosphate permease of Escherichia coli analysed by phoA and lacZ protein fusionsMolecular Microbiology, 1988
- [1] Production of single-stranded plasmid DNAPublished by Elsevier ,1987
- Hypothesis about the function of membrane-buried proline residues in transport proteins.Proceedings of the National Academy of Sciences, 1986
- DNA sequencing with chain-terminating inhibitorsProceedings of the National Academy of Sciences, 1977
- Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteinsBiochemistry, 1974
- Uptake of amino acids by Salmonella typhimuriumArchives of Biochemistry and Biophysics, 1964
- Studies on tryptophan permease in Escherichia coliBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963