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Literature DB >> 8226700

Site-directed mutagenesis reveals the importance of conserved charged residues for the transport activity of the PheP permease of Escherichia coli.

Abstract

Site-directed mutagenesis has been used to identify a number of charged residues essential for the transport activity of the PheP protein. These residues are highly conserved in the cluster of amino acid transporters. However, some other conserved residues and a number of aromatic residues have been shown not to be essential for transport activity.

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Year: 1993 PMID： 8226700 PMCID： PMC206900 DOI： 10.1128/jb.175.22.7500-7504.1993

Source DB: PubMed Journal: J Bacteriol ISSN： 0021-9193 Impact factor: 3.490

21 in total

1. Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes.

Authors: D L Daniels; G Plunkett; V Burland; F R Blattner
Journal: Science Date: 1992-08-07 Impact factor: 47.728

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

Authors: J P Sarsero; P J Wookey; P Gollnick; C Yanofsky; A J Pittard
Journal: J Bacteriol Date: 1991-05 Impact factor: 3.490

3. Nucleotide sequence of the aroP gene encoding the general aromatic amino acid transport protein of Escherichia coli K-12: homology with yeast transport proteins.

Authors: N Honoré; S T Cole
Journal: Nucleic Acids Res Date: 1990-02-11 Impact factor: 16.971

4. GAP1, the general amino acid permease gene of Saccharomyces cerevisiae. Nucleotide sequence, protein similarity with the other bakers yeast amino acid permeases, and nitrogen catabolite repression.

Authors: J C Jauniaux; M Grenson
Journal: Eur J Biochem Date: 1990-05-31

5. Cloning and sequencing of the pheP gene, which encodes the phenylalanine-specific transport system of Escherichia coli.

Authors: J Pi; P J Wookey; A J Pittard
Journal: J Bacteriol Date: 1991-06 Impact factor: 3.490

6. The interaction between aspartic acid 237 and lysine 358 in the lactose carrier of Escherichia coli.

Authors: S C King; C L Hansen; T H Wilson
Journal: Biochim Biophys Acta Date: 1991-02-25

7. The histidine permease gene (HIP1) of Saccharomyces cerevisiae.

Authors: J Tanaka; G R Fink
Journal: Gene Date: 1985 Impact factor: 3.688

8. Molecular characterization of the CAN1 locus in Saccharomyces cerevisiae. A transmembrane protein without N-terminal hydrophobic signal sequence.

Authors: W Hoffmann
Journal: J Biol Chem Date: 1985-09-25 Impact factor: 5.157

9. The lysP gene encodes the lysine-specific permease.

Authors: C Steffes; J Ellis; J Wu; B P Rosen
Journal: J Bacteriol Date: 1992-05 Impact factor: 3.490

10. Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: similarities between CAN1, HIP1 and PUT4 permeases.

Authors: M Vandenbol; J C Jauniaux; M Grenson
Journal: Gene Date: 1989-11-15 Impact factor: 3.688

10 in total

8. Identification of a receptor subunit and putative ligand-binding residues involved in the Bacillus megaterium QM B1551 spore germination response to glucose.

Authors: Graham Christie; Hansjörg Götzke; Christopher R Lowe
Journal: J Bacteriol Date: 2010-06-25 Impact factor: 3.490

9. Study of second-site suppression in the pheP gene for the phenylalanine transporter of Escherichia coli.

Authors: Jing Pi; H Chow; A J Pittard
Journal: J Bacteriol Date: 2002-11 Impact factor: 3.490

10. Membrane topology of the Escherichia coli gamma-aminobutyrate transporter: implications on the topography and mechanism of prokaryotic and eukaryotic transporters from the APC superfamily.

Authors: L A Hu; S C King
Journal: Biochem J Date: 1998-11-15 Impact factor: 3.857

10 in total

Site-directed mutagenesis reveals the importance of conserved charged residues for the transport activity of the PheP permease of Escherichia coli.

1. Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes.

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

3. Nucleotide sequence of the aroP gene encoding the general aromatic amino acid transport protein of Escherichia coli K-12: homology with yeast transport proteins.

4. GAP1, the general amino acid permease gene of Saccharomyces cerevisiae. Nucleotide sequence, protein similarity with the other bakers yeast amino acid permeases, and nitrogen catabolite repression.

5. Cloning and sequencing of the pheP gene, which encodes the phenylalanine-specific transport system of Escherichia coli.

6. The interaction between aspartic acid 237 and lysine 358 in the lactose carrier of Escherichia coli.

7. The histidine permease gene (HIP1) of Saccharomyces cerevisiae.

8. Molecular characterization of the CAN1 locus in Saccharomyces cerevisiae. A transmembrane protein without N-terminal hydrophobic signal sequence.

9. The lysP gene encodes the lysine-specific permease.

10. Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: similarities between CAN1, HIP1 and PUT4 permeases.

1. ANT1, an aromatic and neutral amino acid transporter in Arabidopsis.

2. A study of AroP-PheP chimeric proteins and identification of a residue involved in tryptophan transport.

3. Putative interhelical interactions within the PheP protein revealed by second-site suppressor analysis.

4. Functional consequences of changing proline residues in the phenylalanine-specific permease of Escherichia coli.

Review 5. Linkage map of Escherichia coli K-12, edition 10: the traditional map.

6. Topology of the phenylalanine-specific permease of Escherichia coli.

7. A topological model for the general aromatic amino acid permease, AroP, of Escherichia coli.

8. Identification of a receptor subunit and putative ligand-binding residues involved in the Bacillus megaterium QM B1551 spore germination response to glucose.

9. Study of second-site suppression in the pheP gene for the phenylalanine transporter of Escherichia coli.

10. Membrane topology of the Escherichia coli gamma-aminobutyrate transporter: implications on the topography and mechanism of prokaryotic and eukaryotic transporters from the APC superfamily.