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Volumn 185, Issue 21, 2003, Pages 6225-6232

Putative Interhelical Interactions within the PheP Protein Revealed by Second-Site Suppressor Analysis

(3)  Dogovski, C a   Pi, J a   Pittard, A J a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMINO ACID TRANSPORTER; BACTERIAL PROTEIN; GLYCINE; MEMBRANE PROTEIN; MUTANT PROTEIN; PHENYLALANINE; PHEP PROTEIN; POLYAMINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 0142183490     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.21.6225-6232.2003     Document Type: Article
Times cited : (10)

References (27)
  • 1
    • 0034029583 scopus 로고    scopus 로고
    • A study of AroP-PheP chimeric proteins and identification of a residue involved in tryptophan transport
    • Cosgriff, A. J., 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.J.1    Brasier, G.2    Pi, J.3    Dogovski, C.4    Sarsero, J.P.5    Pittard, A.J.6
  • 2
    • 0022995724 scopus 로고
    • Amino acid composition of the membrane and aqueous domains of integral membrane proteins
    • Deber, C. M., C. J. Brandl, R. B. Deber, L. C. Hsu, and X. K. Young. 1986. Amino acid composition of the membrane and aqueous domains of integral membrane proteins. Arch. Biochem. Biophys. 251:68-76.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 68-76
    • Deber, C.M.1    Brandl, C.J.2    Deber, R.B.3    Hsu, L.C.4    Young, X.K.5
  • 4
    • 0019464222 scopus 로고
    • The spontaneous insertion of proteins into and across membranes: The helical hairpin hypothesis
    • Engelman, D. M., and T. A. Steitz. 1981. The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell 23:411-422.
    • (1981) Cell , vol.23 , pp. 411-422
    • Engelman, D.M.1    Steitz, T.A.2
  • 5
    • 0025142363 scopus 로고
    • Initial steps in membrane protein insertion. Bacteriophage M13 procoat binds to the membrane surface by electrostatic interaction
    • Gallusser, A., and A. Kuhn. 1990. Initial steps in membrane protein insertion. Bacteriophage M13 procoat binds to the membrane surface by electrostatic interaction. EMBO J. 9:2723-2729.
    • (1990) EMBO J. , vol.9 , pp. 2723-2729
    • Gallusser, A.1    Kuhn, A.2
  • 6
  • 7
    • 0028815284 scopus 로고
    • Forces and factors that contribute to the structural stability of membrane proteins
    • Haltia, T., and E. Freire. 1995. Forces and factors that contribute to the structural stability of membrane proteins. Biochim. Biophys. Acta 1228:1-27.
    • (1995) Biochim. Biophys. Acta , vol.1228 , pp. 1-27
    • Haltia, T.1    Freire, E.2
  • 8
    • 0025812217 scopus 로고
    • In vivo analysis of integration of membrane proteins in Escherichia coli
    • Ito, K., and Y. Akiyama. 1991. In vivo analysis of integration of membrane proteins in Escherichia coli. Mol. Microbiol. 55:2243-2253.
    • (1991) Mol. Microbiol. , vol.55 , pp. 2243-2253
    • Ito, K.1    Akiyama, Y.2
  • 9
    • 0033886562 scopus 로고    scopus 로고
    • The amino acid/polyamine/organocation (APC) superfamily of transporters specific for amino acids, polyamines and organocations
    • Jack, D. L., I. T. Paulsen, and M. H. Saier. 2000. The amino acid/polyamine/organocation (APC) superfamily of transporters specific for amino acids, polyamines and organocations. Microbiology 146:1797-1814.
    • (2000) Microbiology , vol.146 , pp. 1797-1814
    • Jack, D.L.1    Paulsen, I.T.2    Saier, M.H.3
  • 10
    • 0032817780 scopus 로고    scopus 로고
    • Helix packing in polytopic membrane proteins: Role of glycine in transmembrane helix association
    • Javadpour, M. M., M Eilers, M. Groesbeek, and S. O. Smith. 1999. Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association. Biophys. J. 77:1609-1618.
    • (1999) Biophys. J. , vol.77 , pp. 1609-1618
    • Javadpour, M.M.1    Eilers, M.2    Groesbeek, M.3    Smith, S.O.4
  • 11
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins
    • Landolt-Marticorena, C., K. A. Williams, C. M. Deber, and R. A. Reithmeier. 1993. Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins. J. Mol. Biol. 229:602-608.
    • (1993) J. Mol. Biol. , vol.229 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reithmeier, R.A.4
  • 13
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K. R., J. H. Prestegard, and D. M. Engelman. 1997. A transmembrane helix dimer: structure and implications. Science 276:131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 14
    • 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. Cohen. 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    Cohen, M.3
  • 15
    • 0142244827 scopus 로고
    • Ph. D thesis. University of Melbourne, Melbourne, Australia
    • Pi, J. 1991. Ph. D thesis. University of Melbourne, Melbourne, Australia.
    • (1991)
    • Pi, J.1
  • 16
    • 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., 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    Pittard, A.J.2
  • 17
    • 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
  • 18
    • 0036838011 scopus 로고    scopus 로고
    • Study of second-site suppression in the pheP gene for the phenylalanine transporter of Escherichia coli
    • Pi, J., H. Chow, and A. J. Pittard. 2002. Study of second-site suppression in the pheP gene for the phenylalanine transporter of Escherichia coli. J. Bacteriol. 184:5842-5847.
    • (2002) J. Bacteriol. , vol.184 , pp. 5842-5847
    • Pi, J.1    Chow, H.2    Pittard, A.J.3
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerisation: The two stage model
    • Popot, J. L., and D. M. Engelman. 1990. Membrane protein folding and oligomerisation: the two stage model. Biochemistry 29:4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 22
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of α-helices
    • Richardson, J. S., and D. C. Richardson. 1988. Amino acid preferences for specific locations at the ends of α-helices. Science 240:1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 23
    • 0034711953 scopus 로고    scopus 로고
    • The GXXXG motif: A framework for transmembrane helix-helix association
    • Russ, W. P., and D. M. Engelman. 2000. The GXXXG motif: a framework for transmembrane helix-helix association. J. Mol. Biol. 296:911-919.
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 24
    • 0033886560 scopus 로고    scopus 로고
    • Families of transmembrane transporters selective for amino acids and their derivatives
    • Saier, M. H. 2000. Families of transmembrane transporters selective for amino acids and their derivatives. Microbiology 146:1775-1795.
    • (2000) Microbiology , vol.146 , pp. 1775-1795
    • Saier, M.H.1
  • 26
    • 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
  • 27
    • 0021224006 scopus 로고
    • Cloning of the tyrP gene and further characterization of the tyrosine-specific transport protein in Escherichia coli K-12
    • Wookey, P. J., J. Pittard, S. M. Forrest, and B. E. Davidson. 1984. Cloning of the tyrP gene and further characterization of the tyrosine-specific transport protein in Escherichia coli K-12. J. Bacteriol. 160:169-174.
    • (1984) J. Bacteriol. , vol.160 , pp. 169-174
    • Wookey, P.J.1    Pittard, J.2    Forrest, S.M.3    Davidson, B.E.4


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