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Volumn 184, Issue 21, 2002, Pages 5842-5847

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

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; PHENYLALANINE TRANSPORTER; UNCLASSIFIED DRUG;

EID: 0036838011     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.184.21.5842-5847.2002     Document Type: Article
Times cited : (12)

References (15)
  • 1
    • 0034029583 scopus 로고    scopus 로고
    • A study of AroP-PheP chimeric proteins and identification of a residue involved in tryptophan transport
    • Cosgriff, A., G. Brasier, J. Pi, C. Dogovski, J. P. Sarsero, and A. J. Pittard. 2000. A study of AroP-PheP chimeric proteins and identification of a residue involved in tryptophan transport. J. Bacteriol. 182:2207-2217.
    • (2000) J. Bacteriol. , vol.182 , pp. 2207-2217
    • Cosgriff, A.1    Brasier, G.2    Pi, J.3    Dogovski, C.4    Sarsero, J.P.5    Pittard, A.J.6
  • 2
    • 0032031494 scopus 로고    scopus 로고
    • Functional sensitivity of polar surfaces on transmembrane helix 8 and cytoplasmic loop 8-9 of the Escherichia coli GABA (4-aminobutyrate) transporter encoded by gabP: Mutagenic analysis of a consensus amphipathic region found in transporters from bacteria to mammals
    • Hu, L. A., and S. C. King. 1998. Functional sensitivity of polar surfaces on transmembrane helix 8 and cytoplasmic loop 8-9 of the Escherichia coli GABA (4-aminobutyrate) transporter encoded by gabP: mutagenic analysis of a consensus amphipathic region found in transporters from bacteria to mammals. Biochem. J. 330:771-776.
    • (1998) Biochem. J. , vol.330 , pp. 771-776
    • Hu, L.A.1    King, S.C.2
  • 3
    • 0032533163 scopus 로고    scopus 로고
    • Membrane topology of the Escherichia coli gamma-aminobutyrate transporter: Implications on the topography and mechanism of prokaryotic transporters from the APC superfamily
    • Hu, L. A., and S. C. King. 1998. Membrane topology of the Escherichia coli gamma-aminobutyrate transporter: implications on the topography and mechanism of prokaryotic transporters from the APC superfamily. Biochem J. 336:69-76.
    • (1998) Biochem. J. , vol.336 , pp. 69-76
    • Hu, L.A.1    King, S.C.2
  • 4
    • 0025369088 scopus 로고
    • In vivo cloning and characterization of gabCTDP gene cluster of Escherichia coli K-12
    • Metzer, E., and Y. S. Halpern. 1990. In vivo cloning and characterization of gabCTDP gene cluster of Escherichia coli K-12. J. Bacteriol. 172:3250-3256.
    • (1990) J. Bacteriol. , vol.172 , pp. 3250-3256
    • Metzer, E.1    Halpern, Y.S.2
  • 5
    • 0000498179 scopus 로고
    • Sur la biosynthese de la β-galactosidase (lactase) chez Escherichia coli. La specificite de l'induction
    • Monod, J., G. Cohen-Bazire, and M. Cohn. 1951. Sur la biosynthese de la β-galactosidase (lactase) chez Escherichia coli. La specificite de l'induction. Biochim. Biophys. Acta 7:585-599.
    • (1951) Biochim. Biophys. Acta , vol.7 , pp. 585-599
    • Monod, J.1    Cohen-Bazire, G.2    Cohn, M.3
  • 6
    • 15444350660 scopus 로고    scopus 로고
    • Functional consequences of changing proline residues in the phenylalanine-specific permease of Escherichia coli
    • Pi, J., C. Dogovski, and A. J. Pittard. 1998. Functional consequences of changing proline residues in the phenylalanine-specific permease of Escherichia coli. J. Bacteriol. 180:5515-5519.
    • (1998) J. Bacteriol. , vol.180 , pp. 5515-5519
    • Pi, J.1    Dogovski, C.2    Pittard, A.J.3
  • 7
    • 0029966330 scopus 로고    scopus 로고
    • Topology of the phenylalanine-specific permease of Escherichia coli
    • Pi, J., and A. J. Pittard. 1996. Topology of the phenylalanine-specific permease of Escherichia coli. J. Bacteriol. 178:2650-2655.
    • (1996) J. Bacteriol. , vol.178 , pp. 2650-2655
    • Pi, J.1    Pittard, A.J.2
  • 8
    • 0025766783 scopus 로고
    • Cloning and sequencing of the pheP gene, which encodes the phenylalanine-specific transport system of Escherichia coli
    • Pi, J., P. J. Wookey, and A. J. Pittard. 1991. Cloning and sequencing of the pheP gene, which encodes the phenylalanine-specific transport system of Escherichia coli. J. Bacteriol. 173:3622-3629.
    • (1991) J. Bacteriol. , vol.173 , pp. 3622-3629
    • Pi, J.1    Wookey, P.J.2    Pittard, A.J.3
  • 9
    • 0027526962 scopus 로고
    • Site-directed mutagenesis reveals the importance of conserved charged residues for the transport activity of the PheP permease of Escherichia coli
    • Pi, J., P. J. Wookey, and A. J. Pittard. 1993. Site-directed mutagenesis reveals the importance of conserved charged residues for the transport activity of the PheP permease of Escherichia coli. J. Bacteriol. 175:7500-7504.
    • (1993) J. Bacteriol. , vol.175 , pp. 7500-7504
    • Pi, J.1    Wookey, P.J.2    Pittard, A.J.3
  • 10
    • 0003716359 scopus 로고
    • p. I-A-ii-1. Elsevier Science Publishers, B. V., Amsterdam, The Netherlands
    • Pouwels, P. H., B. E. Enger-Valk, and W. J. Brammar. 1985. Cloning vectors, p. I-A-ii-1. Elsevier Science Publishers, B. V., Amsterdam, The Netherlands.
    • (1985) Cloning vectors
    • Pouwels, P.H.1    Enger-Valk, B.E.2    Brammar, W.J.3
  • 11
    • 0027382884 scopus 로고
    • Properties of interacting aspartic acid and lysine residues in the lactose permease of Escherichia coli
    • Sahin-Toth, M., and H. R. Kaback. 1993. Properties of interacting aspartic acid and lysine residues in the lactose permease of Escherichia coli. Biochemistry 32:10027-10035.
    • (1993) Biochemistry , vol.32 , pp. 10027-10035
    • Sahin-Toth, M.1    Kaback, H.R.2
  • 12
    • 0033431036 scopus 로고    scopus 로고
    • A conserved serine-rich stretch in the glutamate transporter family forms a substrate-sensitive reentrant loop
    • Slotboom, D. J., I. Sobczak, W. N. Konings, and J. S. Lolkema. 1999. A conserved serine-rich stretch in the glutamate transporter family forms a substrate-sensitive reentrant loop. Proc. Natl. Acad. Sci. USA 96:14282-14287.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14282-14287
    • Slotboom, D.J.1    Sobczak, I.2    Konings, W.N.3    Lolkema, J.S.4
  • 13
    • 0023929638 scopus 로고
    • A simple and rapid method for the selection of oligodeoxynucleotide-directed mutants
    • Vandeyar, M. A., M. P. Weiner, C. J. Hutton, and C. A. Batt. 1988. A simple and rapid method for the selection of oligodeoxynucleotide-directed mutants. Gene 65:129-133.
    • (1988) Gene , vol.65 , pp. 129-133
    • Vandeyar, M.A.1    Weiner, M.P.2    Hutton, C.J.3    Batt, C.A.4
  • 14
    • 0034604695 scopus 로고    scopus 로고
    • Close approximation of putative alpha-helices II, IV, VII, X, and XI in the translocation pathway of the lactose transport protein of Streptococcus thermophilus
    • Veenhoff, L. M., E. R. Geertsma, J. Knol, and B. Poolman. 2000. Close approximation of putative alpha-helices II, IV, VII, X, and XI in the translocation pathway of the lactose transport protein of Streptococcus thermophilus. J. Biol. Chem. 275:23834-23840.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23834-23840
    • Veenhoff, L.M.1    Geertsma, E.R.2    Knol, J.3    Poolman, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.