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

doi:10.1128/jb.173.10.3231-3234.1991

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

Biological Sciences

Stanford University

Research output: Contribution to journal › Article › peer-review

44 Scopus citations

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.

Original language	English
Pages (from-to)	3231-3234
Number of pages	4
Journal	Journal of Bacteriology
Volume	173
Issue number	10
DOIs	https://doi.org/10.1128/jb.173.10.3231-3234.1991
State	Published - 1991

Access to Document

10.1128/jb.173.10.3231-3234.1991

Cite this

@article{0883fadca73c4b8c8d321a87203cb517,

title = "A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli",

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.",

author = "Sarsero, \{J. P.\} and Wookey, \{P. J.\} and P. Gollnick and C. Yanofsky and Pittard, \{A. J.\}",

year = "1991",

doi = "10.1128/jb.173.10.3231-3234.1991",

language = "English",

volume = "173",

pages = "3231--3234",

journal = "Journal of Bacteriology",

issn = "0021-9193",

publisher = "American Society for Microbiology",

number = "10",

}

TY - JOUR

T1 - A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli

AU - Sarsero, J. P.

AU - Wookey, P. J.

AU - Gollnick, P.

AU - Yanofsky, C.

AU - Pittard, A. J.

PY - 1991

Y1 - 1991

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0025810777

U2 - 10.1128/jb.173.10.3231-3234.1991

DO - 10.1128/jb.173.10.3231-3234.1991

M3 - Article

C2 - 2022620

AN - SCOPUS:0025810777

SN - 0021-9193

VL - 173

SP - 3231

EP - 3234

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 10

ER -

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

Abstract

Access to Document

Other files and links

Fingerprint

Cite this