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Volumn 213, Issue 2, 2006, Pages 119-133

Secondary transport of amino acids in prokaryotes

Author keywords

Amino acid transport; Secondary transport; Sodium solute symport

Indexed keywords

AMINO ACID;

EID: 34247248894     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00232-006-0880-x     Document Type: Review
Times cited : (18)

References (95)
  • 1
    • 0030063772 scopus 로고    scopus 로고
    • Exchange of aspartate and alanine. Mechanism for development of a proton-motive force in bacteria
    • Abe, K., Hayashi, H., Maloney, P.C. 1996. Exchange of aspartate and alanine. Mechanism for development of a proton-motive force in bacteria. J. Biol. Chem. 271:3079-3084
    • (1996) J. Biol. Chem , vol.271 , pp. 3079-3084
    • Abe, K.1    Hayashi, H.2    Maloney, P.C.3
  • 2
    • 0036098106 scopus 로고    scopus 로고
    • Plasmidencoded asp operon confers a proton motive metabolic cycle catalyzed by an aspartate-alanine exchange reaction
    • Abe, K., Ohnishi, F., Yagi, K., Nakajima, T., Higuchi, T., Sano, M., Machida, M., Sarker, R.I., Maloney, P.C. 2002. Plasmidencoded asp operon confers a proton motive metabolic cycle catalyzed by an aspartate-alanine exchange reaction. J. Bacteriol. 184:2906-2913
    • (2002) J. Bacteriol , vol.184 , pp. 2906-2913
    • Abe, K.1    Ohnishi, F.2    Yagi, K.3    Nakajima, T.4    Higuchi, T.5    Sano, M.6    Machida, M.7    Sarker, R.I.8    Maloney, P.C.9
  • 3
    • 0041353145 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease of Escherichia coli
    • Abramson, J., Smirnova, I., Kasho, V., Verner, G., Kaback, H.R., Iwata, S. 2003. Structure and mechanism of the lactose permease of Escherichia coli. Science 301:610-615
    • (2003) Science , vol.301 , pp. 610-615
    • Abramson, J.1    Smirnova, I.2    Kasho, V.3    Verner, G.4    Kaback, H.R.5    Iwata, S.6
  • 5
    • 0032912746 scopus 로고    scopus 로고
    • Impact of the high-affinity proline permease gene (putP) on the virulence of Staphylococcus aureus in experimental endocarditis
    • Bayer, A.S., Coulter, S.N., Stover, C.K., Schwan, W.R. 1999. Impact of the high-affinity proline permease gene (putP) on the virulence of Staphylococcus aureus in experimental endocarditis. Infect Immun. 67:740-744
    • (1999) Infect Immun , vol.67 , pp. 740-744
    • Bayer, A.S.1    Coulter, S.N.2    Stover, C.K.3    Schwan, W.R.4
  • 6
    • 0023825249 scopus 로고
    • Bioenergetic coupling to protonmotive force: Should we be considering hydronium ion coordination and not group protonation?
    • Boyer, P.D. 1988. Bioenergetic coupling to protonmotive force: should we be considering hydronium ion coordination and not group protonation? Trends Biochem. Sci. 13:5-7
    • (1988) Trends Biochem. Sci , vol.13 , pp. 5-7
    • Boyer, P.D.1
  • 7
    • 0035823075 scopus 로고    scopus 로고
    • Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters
    • Chang, G., Roth, C.B. 2001. Structure of MsbA from E. coli: A homolog of the multidrug resistance ATP binding cassette (ABC) transporters. Science 293:1793-1800
    • (2001) Science , vol.293 , pp. 1793-1800
    • Chang, G.1    Roth, C.B.2
  • 9
    • 0012151584 scopus 로고    scopus 로고
    • Identification of a major facilitator protein from Escherichia coli involved in efflux of metabolites of the cysteine pathway
    • Dassler, T., Maier, T., Winterhalter, C., Böck, A. 2000. Identification of a major facilitator protein from Escherichia coli involved in efflux of metabolites of the cysteine pathway. Mol. Microbiol. 36:1101-1112
    • (2000) Mol. Microbiol , vol.36 , pp. 1101-1112
    • Dassler, T.1    Maier, T.2    Winterhalter, C.3    Böck, A.4
  • 10
    • 3943062954 scopus 로고    scopus 로고
    • ATP-binding cassette transporters in bacteria
    • Davidson, A.L., Chen, J. 2004. ATP-binding cassette transporters in bacteria. Annu. Rev. Biochem. 73:241-268
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 241-268
    • Davidson, A.L.1    Chen, J.2
  • 12
    • 34247205611 scopus 로고    scopus 로고
    • DeLano, W.L. 2002. The PyMOL molecular graphics system. http://www.pymol.org
    • (2002)
    • DeLano, W.L.1
  • 13
    • 0022974409 scopus 로고
    • Proline transport in Salmonella typhimurium: PutP permease mutants with altered substrate specificity
    • Dila, D.K., Maloy, S.R. 1986. Proline transport in Salmonella typhimurium: putP permease mutants with altered substrate specificity. J. Bacteriol. 168:590-594
    • (1986) J. Bacteriol , vol.168 , pp. 590-594
    • Dila, D.K.1    Maloy, S.R.2
  • 14
    • 0142183490 scopus 로고    scopus 로고
    • Putative interhelical interactions within the PheP protein revealed by second-site suppressor analysis
    • Dogovski, C., Pi, J., Pittard, A.J. 2003. Putative interhelical interactions within the PheP protein revealed by second-site suppressor analysis. J. Bacteriol. 185:6225-6232
    • (2003) J. Bacteriol , vol.185 , pp. 6225-6232
    • Dogovski, C.1    Pi, J.2    Pittard, A.J.3
  • 15
    • 10044292705 scopus 로고    scopus 로고
    • Insights into the genomic basis of niche specificity of Pseudomonas putida KT2440
    • dos Santos, V.A.P., Heim, S., Moore, E.R., Stratz, M., Timmis, K.N. 2004. Insights into the genomic basis of niche specificity of Pseudomonas putida KT2440. Environ. Microbiol. 6:1264-1286
    • (2004) Environ. Microbiol , vol.6 , pp. 1264-1286
    • dos Santos, V.A.P.1    Heim, S.2    Moore, E.R.3    Stratz, M.4    Timmis, K.N.5
  • 17
    • 0034255851 scopus 로고    scopus 로고
    • Diversity of transport mechanisms: Common structural principles
    • Driessen, A.J., Rosen, B.P., Konings, W.N. 2000. Diversity of transport mechanisms: common structural principles. Trends Biochem. Sci. 25:397-401
    • (2000) Trends Biochem. Sci , vol.25 , pp. 397-401
    • Driessen, A.J.1    Rosen, B.P.2    Konings, W.N.3
  • 18
    • 0041335542 scopus 로고    scopus 로고
    • New ubiquitous translocators: Amino acid export by Corynebacterium glutamicum and Escherichia coli
    • Eggeling, L., Sahm, H. 2003. New ubiquitous translocators: amino acid export by Corynebacterium glutamicum and Escherichia coli. Arch. Microbiol. 180:155-160
    • (2003) Arch. Microbiol , vol.180 , pp. 155-160
    • Eggeling, L.1    Sahm, H.2
  • 19
    • 0037312795 scopus 로고    scopus 로고
    • YfiK from Escherichia coli promotes export of O-acetylserine and cysteine
    • Franke, I., Resch, A., Dassler, T., Maier, T., Böck, A. 2003. YfiK from Escherichia coli promotes export of O-acetylserine and cysteine. J. Bacteriol. 185:1161-1166
    • (2003) J. Bacteriol , vol.185 , pp. 1161-1166
    • Franke, I.1    Resch, A.2    Dassler, T.3    Maier, T.4    Böck, A.5
  • 21
    • 0029869003 scopus 로고    scopus 로고
    • Purification and reconstitution of the glutamate carrier GltT of the thermophilic bacterium Bacillus stearothermophilus
    • Gaillard, I., Slotboom, D.J., Knol, J., Lolkema, J.S., Konings, W.N. 1996. Purification and reconstitution of the glutamate carrier GltT of the thermophilic bacterium Bacillus stearothermophilus. Biochemistry 35:6150-6156
    • (1996) Biochemistry , vol.35 , pp. 6150-6156
    • Gaillard, I.1    Slotboom, D.J.2    Knol, J.3    Lolkema, J.S.4    Konings, W.N.5
  • 22
    • 3843065666 scopus 로고    scopus 로고
    • Membrane topology of system xc- light subunit reveals a re-entrant loop with substrate-restricted accessibility
    • Gasol, E., Jimenez-Vidal, M., Chillaron, J., Zorzano, A., Palacin, M. 2004. Membrane topology of system xc- light subunit reveals a re-entrant loop with substrate-restricted accessibility. J. Biol. Chem. 279:31228-31236
    • (2004) J. Biol. Chem , vol.279 , pp. 31228-31236
    • Gasol, E.1    Jimenez-Vidal, M.2    Chillaron, J.3    Zorzano, A.4    Palacin, M.5
  • 24
    • 28544453561 scopus 로고    scopus 로고
    • Principles of selective ion transport in channels and pumps
    • Gouaux, E., MacKinnon, R. 2005. Principles of selective ion transport in channels and pumps. Science 310:1461-1465
    • (2005) Science , vol.310 , pp. 1461-1465
    • Gouaux, E.1    MacKinnon, R.2
  • 27
    • 23044451841 scopus 로고    scopus 로고
    • Formation of an antiparallel, intermolecular coiled coil is associated with in vivo dimerization of osmosensor and osmoprotectant transporter ProP in Escherichia coli
    • Hillar, A., Culham, D.E., Vernikovska, Y.I., Wood, J.M., Boggs, J.M. 2005. Formation of an antiparallel, intermolecular coiled coil is associated with in vivo dimerization of osmosensor and osmoprotectant transporter ProP in Escherichia coli. Biochemistry 44:10170-10180
    • (2005) Biochemistry , vol.44 , pp. 10170-10180
    • Hillar, A.1    Culham, D.E.2    Vernikovska, Y.I.3    Wood, J.M.4    Boggs, J.M.5
  • 28
    • 0348224027 scopus 로고    scopus 로고
    • Detection of alpha-helical coiled-coil dimer formation by spin-labeled synthetic peptides: A model parallel coiled-coil peptide and the antiparallel coiled coil formed by a replica of the ProP C-terminus
    • Hillar, A., Tripet, B., Zoetewey, D., Wood, J.M., Hodges, R.S., Boggs, J.M. 2003. Detection of alpha-helical coiled-coil dimer formation by spin-labeled synthetic peptides: a model parallel coiled-coil peptide and the antiparallel coiled coil formed by a replica of the ProP C-terminus. Biochemistry. 42:15170-15178
    • (2003) Biochemistry , vol.42 , pp. 15170-15178
    • Hillar, A.1    Tripet, B.2    Zoetewey, D.3    Wood, J.M.4    Hodges, R.S.5    Boggs, J.M.6
  • 29
    • 0041489951 scopus 로고    scopus 로고
    • Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli
    • Huang, Y., Lemieux, M.J., Song, J., Auer, M., Wang, D.N. 2003. Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli. Science 301:616-620
    • (2003) Science , vol.301 , pp. 616-620
    • Huang, Y.1    Lemieux, M.J.2    Song, J.3    Auer, M.4    Wang, D.N.5
  • 30
    • 0242659209 scopus 로고    scopus 로고
    • Arginine-agmatine antiporter in extreme acid resistance in Escherichia coli
    • Iyer, R., Williams, C., Miller, C. 2003. Arginine-agmatine antiporter in extreme acid resistance in Escherichia coli. J. Bacteriol. 185:6556-6561
    • (2003) J. Bacteriol , vol.185 , pp. 6556-6561
    • Iyer, R.1    Williams, C.2    Miller, C.3
  • 31
    • 0033886562 scopus 로고    scopus 로고
    • The amino acid/polyamine/organocation (APC) superfamily of transporters specific for amino acids, polyamines and organocations
    • Jack, D.L., Paulsen, I.T., Saier, M.H. Jr. 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 Jr., M.H.3
  • 32
    • 0037112592 scopus 로고    scopus 로고
    • Distance measurements in the nanometer range by pulse EPR
    • Jeschke, G. 2002. Distance measurements in the nanometer range by pulse EPR. Chemphyschem. 3:927-932
    • (2002) Chemphyschem , vol.3 , pp. 927-932
    • Jeschke, G.1
  • 34
    • 0032321679 scopus 로고    scopus 로고
    • +/solute cotransporter family
    • +/solute cotransporter family. Biochim. Biophys. Acta. 1365:60-64
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 60-64
    • Jung, H.1
  • 35
    • 0037010179 scopus 로고    scopus 로고
    • The sodium/substrate symporter family: Structural and functional features
    • Jung, H. 2002. The sodium/substrate symporter family: structural and functional features. FEBS Lett. 529:73-77
    • (2002) FEBS Lett , vol.529 , pp. 73-77
    • Jung, H.1
  • 36
    • 0035342629 scopus 로고    scopus 로고
    • +/solute symport in prokaryotes
    • +/solute symport in prokaryotes. Biochim. Biophys. Acta. 1505:131-143
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 131-143
    • Jung, H.1
  • 38
    • 1342282979 scopus 로고    scopus 로고
    • Identification of an additional interaction domain in transmembrane domains 11 and 12 that supports oligomer formation in the human serotonin transporter
    • Just, H., Sitte, H.H., Schmid, J.A., Freissmuth, M., Kudlacek, O. 2004. Identification of an additional interaction domain in transmembrane domains 11 and 12 that supports oligomer formation in the human serotonin transporter. J. Biol. Chem. 279:6650-6657
    • (2004) J. Biol. Chem , vol.279 , pp. 6650-6657
    • Just, H.1    Sitte, H.H.2    Schmid, J.A.3    Freissmuth, M.4    Kudlacek, O.5
  • 39
    • 20444419395 scopus 로고    scopus 로고
    • Structure and mechanism of the lactose permease
    • Kaback, H.R. 2005. Structure and mechanism of the lactose permease. C. R. Biol. 328:557-567
    • (2005) C. R. Biol , vol.328 , pp. 557-567
    • Kaback, H.R.1
  • 40
    • 7244223160 scopus 로고    scopus 로고
    • Accessing a transporter structure
    • Kavanaugh, M.P. 2004. Accessing a transporter structure. Nature 431:752-753
    • (2004) Nature , vol.431 , pp. 752-753
    • Kavanaugh, M.P.1
  • 41
    • 0034889137 scopus 로고    scopus 로고
    • The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea
    • Kelly, D.J., Thomas, G.H. 2001. The tripartite ATP-independent periplasmic (TRAP) transporters of bacteria and archaea. FEMS Microbiol. Rev. 25:405-424
    • (2001) FEMS Microbiol. Rev , vol.25 , pp. 405-424
    • Kelly, D.J.1    Thomas, G.H.2
  • 42
    • 26944450526 scopus 로고    scopus 로고
    • Intramolecular crosslinking in a bacterial homolog of mammalian SLC6 neurotransmitter transporters suggests an evolutionary conserved role of transmembrane segments 7 and 8
    • Kniaze., J., Loland, C.J., Goldberg, N., Quick, M., Das, S., Sitte, H.H., Javitch, J.A., Gether, U. 2005. Intramolecular crosslinking in a bacterial homolog of mammalian SLC6 neurotransmitter transporters suggests an evolutionary conserved role of transmembrane segments 7 and 8. Neuropharmacology 49:715-723
    • (2005) Neuropharmacology , vol.49 , pp. 715-723
    • Kniaze, J.1    Loland, C.J.2    Goldberg, N.3    Quick, M.4    Das, S.5    Sitte, H.H.6    Javitch, J.A.7    Gether, U.8
  • 43
    • 33645693765 scopus 로고    scopus 로고
    • Transition in the temperature-dependence of GFP fluorescence: From proton wires to proton exit
    • Leiderman, P., Huppert, D., Agmon, N. 2006. Transition in the temperature-dependence of GFP fluorescence: from proton wires to proton exit. Biophys. J 90:1009-1018
    • (2006) Biophys. J , vol.90 , pp. 1009-1018
    • Leiderman, P.1    Huppert, D.2    Agmon, N.3
  • 44
    • 0034853645 scopus 로고    scopus 로고
    • Substrate recognition by proline permease in Salmonella
    • Liao, M.K., Maloy, S. 2001. Substrate recognition by proline permease in Salmonella. Amino Acids 21:161-174
    • (2001) Amino Acids , vol.21 , pp. 161-174
    • Liao, M.K.1    Maloy, S.2
  • 45
    • 0029073161 scopus 로고
    • Comparative analysis of extreme acid survival in Salmonella typhimurium, Shigella flexneri, and Escherichia coli
    • Lin, J., Lee, I.S., Frey, J., Slonczewski, J.L., Foster, J.W. 1995. Comparative analysis of extreme acid survival in Salmonella typhimurium, Shigella flexneri, and Escherichia coli. J. Bacteriol. 177:4097-4104
    • (1995) J. Bacteriol , vol.177 , pp. 4097-4104
    • Lin, J.1    Lee, I.S.2    Frey, J.3    Slonczewski, J.L.4    Foster, J.W.5
  • 46
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD Structure: A framework for ABC transporter architecture and mechanism
    • Locher, K.P., Lee, A.T., Rees, D.C. 2002. The E. coli BtuCD Structure: A framework for ABC transporter architecture and mechanism. Science 296:1091-1098
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 47
    • 0031765884 scopus 로고    scopus 로고
    • Hydropathy profile alignment: A tool to search for structural homologues of membrane proteins
    • Lolkema, J.S., Slotboom, D.J. 1998. Hydropathy profile alignment: a tool to search for structural homologues of membrane proteins. FEMS Microbiol. Rev. 22:305-322
    • (1998) FEMS Microbiol. Rev , vol.22 , pp. 305-322
    • Lolkema, J.S.1    Slotboom, D.J.2
  • 48
    • 0037432531 scopus 로고    scopus 로고
    • Classification of 29 families of secondary transport proteins into a single structural class using hydropathy profile analysis
    • Lolkema, J.S., Slotboom, D.J. 2003. Classification of 29 families of secondary transport proteins into a single structural class using hydropathy profile analysis. J. Mol. Biol. 327:901-909
    • (2003) J. Mol. Biol , vol.327 , pp. 901-909
    • Lolkema, J.S.1    Slotboom, D.J.2
  • 49
    • 18444381459 scopus 로고    scopus 로고
    • Secondary transporters of the 2HCT family contain two homologous domains with inverted membrane topology and trans re-entrant loops
    • Lolkema, J.S., Sobczak, I., Slotboom, D.J. 2005. Secondary transporters of the 2HCT family contain two homologous domains with inverted membrane topology and trans re-entrant loops. FEBS J. 272:2334-2344
    • (2005) FEBS J , vol.272 , pp. 2334-2344
    • Lolkema, J.S.1    Sobczak, I.2    Slotboom, D.J.3
  • 52
    • 0027191082 scopus 로고
    • Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri
    • Molenaar, D., Bosscher, J.S., ten Brink, B., Driessen, A.J., Konings, W.N. 1993. Generation of a proton motive force by histidine decarboxylation and electrogenic histidine/histamine antiport in Lactobacillus buchneri. J. Bacteriol. 175:2864-2870
    • (1993) J. Bacteriol , vol.175 , pp. 2864-2870
    • Molenaar, D.1    Bosscher, J.S.2    ten Brink, B.3    Driessen, A.J.4    Konings, W.N.5
  • 54
    • 0035801845 scopus 로고    scopus 로고
    • Probing of the substrate binding domain of lactose permease by a proton pulse
    • Nachliel, E., Gutman, M. 2001. Probing of the substrate binding domain of lactose permease by a proton pulse. Biochim. Biophys. Acta. 1514:33-50
    • (2001) Biochim. Biophys. Acta , vol.1514 , pp. 33-50
    • Nachliel, E.1    Gutman, M.2
  • 55
    • 0034132251 scopus 로고    scopus 로고
    • Dead-time free measurement of dipole-dipole interactions between electron spins
    • Pannier, M., Veit, S., Godt, A., Jeschke, G., Spiess, H.W. 2000. Dead-time free measurement of dipole-dipole interactions between electron spins. J. Magn. Reson. 142:331-340
    • (2000) J. Magn. Reson , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 56
    • 15444350660 scopus 로고    scopus 로고
    • Functional consequences of changing proline residues in the phenylalanine-specific permease of Escherichia coli
    • Pi, J., Dogovski, C., Pittard, A.J. 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
  • 57
    • 0242290359 scopus 로고    scopus 로고
    • +/proline transporter PutP of Escherichia coli forms part of a conformationally flexible, cytoplasmic exposed aqueous cavity within the membrane
    • +/proline transporter PutP of Escherichia coli forms part of a conformationally flexible, cytoplasmic exposed aqueous cavity within the membrane. J. Biol. Chem. 278:42942-42949
    • (2003) J. Biol. Chem , vol.278 , pp. 42942-42949
    • Pirch, T.1    Landmeier, S.2    Jung, H.3
  • 59
    • 0026015262 scopus 로고
    • Malolactic fermentation: Electrogenic malate uptake and malate/lactate antiport generate metabolic energy
    • Poolman, B., Molenaar, D., Smid, E.J., Ubbink, T., Abee, T., Renault, P.P., Konings, W.N. 1991. Malolactic fermentation: electrogenic malate uptake and malate/lactate antiport generate metabolic energy. J. Bacteriol. 173:6030-6037
    • (1991) J. Bacteriol , vol.173 , pp. 6030-6037
    • Poolman, B.1    Molenaar, D.2    Smid, E.J.3    Ubbink, T.4    Abee, T.5    Renault, P.P.6    Konings, W.N.7
  • 61
    • 0030887995 scopus 로고    scopus 로고
    • +-coupled proline uptake
    • +-coupled proline uptake. Biochemistry 36:4631-4636
    • (1997) Biochemistry , vol.36 , pp. 4631-4636
    • Quick, M.1    Jung, H.2
  • 62
    • 0029957853 scopus 로고    scopus 로고
    • +/proline permease of Escherichia coli is critical for high-affinity proline uptake
    • +/proline permease of Escherichia coli is critical for high-affinity proline uptake. Eur. J. Biochem. 239:732-736
    • (1996) Eur. J. Biochem , vol.239 , pp. 732-736
    • Quick, M.1    Tebbe, S.2    Jung, H.3
  • 63
    • 0035208116 scopus 로고    scopus 로고
    • Identification of genes encoding amino acid permeases by inactivation of selected ORFs from the Synechocystis genomic sequence
    • Quintero, M.J., Montesinos, M.L., Herrero, A., Flores, E. 2001. Identification of genes encoding amino acid permeases by inactivation of selected ORFs from the Synechocystis genomic sequence. Genome Res. 11:2034-2040
    • (2001) Genome Res , vol.11 , pp. 2034-2040
    • Quintero, M.J.1    Montesinos, M.L.2    Herrero, A.3    Flores, E.4
  • 65
    • 0028239439 scopus 로고
    • A functional superfamily of sodium/solute symporters
    • Reizer, J., Reizer, A., Saier, M.H.J. 1994. A functional superfamily of sodium/solute symporters. Biochim. Biophys. Acta. 1197:133-166
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 133-166
    • Reizer, J.1    Reizer, A.2    Saier, M.H.J.3
  • 66
    • 0033821267 scopus 로고    scopus 로고
    • Vectorial metabolism and the evolution of transport systems
    • Saier, M.H. Jr 2000a. Vectorial metabolism and the evolution of transport systems. J. Bacteriol. 182:5029-5035
    • (2000) J. Bacteriol , vol.182 , pp. 5029-5035
    • Saier Jr, M.H.1
  • 67
    • 0033886560 scopus 로고    scopus 로고
    • Families of transmembrane transporters selective for amino acids and their derivatives
    • Saier, M.H. Jr 2000b. Families of transmembrane transporters selective for amino acids and their derivatives. Microbiology 146:1775-1795
    • (2000) Microbiology , vol.146 , pp. 1775-1795
    • Saier Jr, M.H.1
  • 68
    • 0343603660 scopus 로고    scopus 로고
    • A functional-phylogenetic classification system for transmembrane solute transporters
    • Saier, M.H. Jr 2000c. A functional-phylogenetic classification system for transmembrane solute transporters. Microbiol. Mol. Biol. Rev. 64:354-411
    • (2000) Microbiol. Mol. Biol. Rev , vol.64 , pp. 354-411
    • Saier Jr, M.H.1
  • 69
    • 0025810777 scopus 로고
    • A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli
    • Sarsero, J.P., Wookey, P.J., Gollnick, P., Yanofsky, C., Pittard, A.J. 1991. A new family of integral membrane proteins involved in transport of aromatic amino acids in Escherichia coli. J. Bacteriol. 173:3231-3234
    • (1991) J. Bacteriol , vol.173 , pp. 3231-3234
    • Sarsero, J.P.1    Wookey, P.J.2    Gollnick, P.3    Yanofsky, C.4    Pittard, A.J.5
  • 71
    • 1942505301 scopus 로고    scopus 로고
    • Low-proline environments impair growth, proline transport and in vivo survival of Staphylococcus aureus strain-specific putP mutants
    • Schwan, W.R., Wetzel, K.J., Gomez, T.S., Stiles, M.A., Beitlich, B.D., Grunwald, S. 2004. Low-proline environments impair growth, proline transport and in vivo survival of Staphylococcus aureus strain-specific putP mutants. Microbiology 150:1055-1061
    • (2004) Microbiology , vol.150 , pp. 1055-1061
    • Schwan, W.R.1    Wetzel, K.J.2    Gomez, T.S.3    Stiles, M.A.4    Beitlich, B.D.5    Grunwald, S.6
  • 72
    • 0034864184 scopus 로고    scopus 로고
    • L-threonine export: Use of peptides to identify a new translocator from Corynebacterium glutamicum
    • Simic, P., Sahm, H., Eggeling, L. 2001. L-threonine export: use of peptides to identify a new translocator from Corynebacterium glutamicum. J. Bacteriol. 183:5317-5324
    • (2001) J. Bacteriol , vol.183 , pp. 5317-5324
    • Simic, P.1    Sahm, H.2    Eggeling, L.3
  • 73
    • 2542461709 scopus 로고    scopus 로고
    • Sodium-dependent neurotransmitter transporters: Oligomerization as a determinant of transporter function and trafficking
    • Sitte, H.H., Farhan, H., Javitch, J.A. 2004. Sodium-dependent neurotransmitter transporters: oligomerization as a determinant of transporter function and trafficking. Mol. Interv. 4:38-47
    • (2004) Mol. Interv , vol.4 , pp. 38-47
    • Sitte, H.H.1    Farhan, H.2    Javitch, J.A.3
  • 75
    • 0035448934 scopus 로고    scopus 로고
    • Glutamate transporters combine transporter- and channel-like features
    • Slotboom, D.J., Konings, W.N., Lolkema, J.S. 2001. Glutamate transporters combine transporter- and channel-like features. Trends. Biochem. Sci. 26:534-539
    • (2001) Trends. Biochem. Sci , vol.26 , pp. 534-539
    • Slotboom, D.J.1    Konings, W.N.2    Lolkema, J.S.3
  • 76
    • 15744387867 scopus 로고    scopus 로고
    • Structural and mechanistic diversity of secondary transporters
    • Sobczak, I., Lolkema, J.S. 2005. Structural and mechanistic diversity of secondary transporters. Curr. Opin. Microbiol. 8:161-167
    • (2005) Curr. Opin. Microbiol , vol.8 , pp. 161-167
    • Sobczak, I.1    Lolkema, J.S.2
  • 77
    • 1542721578 scopus 로고    scopus 로고
    • Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli
    • Soksawatmaekhin, W., Kuraishi, A., Sakata, K., Kashiwagi, K., Igarashi, K. 2004. Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli. Mol. Microbiol. 51:1401-1412
    • (2004) Mol. Microbiol , vol.51 , pp. 1401-1412
    • Soksawatmaekhin, W.1    Kuraishi, A.2    Sakata, K.3    Kashiwagi, K.4    Igarashi, K.5
  • 78
    • 0031871413 scopus 로고    scopus 로고
    • Osmoregulation of the opuE proline transport gene from Bacillus subtilis: Contributions of the sigma A- and sigma B-dependent stress-responsive promoters
    • Spiegelhalter, F., Bremer, E. 1998. Osmoregulation of the opuE proline transport gene from Bacillus subtilis: contributions of the sigma A- and sigma B-dependent stress-responsive promoters. Mol. Microbiol. 29:285-296
    • (1998) Mol. Microbiol , vol.29 , pp. 285-296
    • Spiegelhalter, F.1    Bremer, E.2
  • 79
    • 8344224484 scopus 로고    scopus 로고
    • Inter- and intra-molecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction
    • Steinhoff, H. J. 2004. Inter- and intra-molecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction. Biol.Chem. 385:913-920
    • (2004) Biol.Chem , vol.385 , pp. 913-920
    • Steinhoff, H.J.1
  • 80
    • 30744445718 scopus 로고    scopus 로고
    • Novel ligands for the extracellular solute receptors of two bacterial TRAP transporters
    • Thomas, G.H., Southworth, T., Leon-Kempis, M.R., Leech, A., Kelly, D.J. 2006. Novel ligands for the extracellular solute receptors of two bacterial TRAP transporters. Microbiology 152:187-198
    • (2006) Microbiology , vol.152 , pp. 187-198
    • Thomas, G.H.1    Southworth, T.2    Leon-Kempis, M.R.3    Leech, A.4    Kelly, D.J.5
  • 81
    • 18944362482 scopus 로고    scopus 로고
    • Characterization of methionine export in Corynebacterium glutamicum
    • Trotschel, C., Deutenberg, D., Bathe, B., Burkovski, A., Kramer, R. 2005. Characterization of methionine export in Corynebacterium glutamicum. J. Bacteriol. 187:3786-3794
    • (2005) J. Bacteriol , vol.187 , pp. 3786-3794
    • Trotschel, C.1    Deutenberg, D.2    Bathe, B.3    Burkovski, A.4    Kramer, R.5
  • 82
    • 29244463867 scopus 로고    scopus 로고
    • The osmotic activation of transporter ProP is tuned by both its C-terminal coiled-coil and osmotically induced changes in phospholipid composition
    • Tsatskis, Y., Khambati, J., Dobson, M., Bogdanov, M., Dowhan, W., Wood, J.M. 2005. The osmotic activation of transporter ProP is tuned by both its C-terminal coiled-coil and osmotically induced changes in phospholipid composition. J. Biol. Chem. 280:41387-41394
    • (2005) J. Biol. Chem , vol.280 , pp. 41387-41394
    • Tsatskis, Y.1    Khambati, J.2    Dobson, M.3    Bogdanov, M.4    Dowhan, W.5    Wood, J.M.6
  • 84
  • 85
    • 0030748256 scopus 로고    scopus 로고
    • von Blohn, C. von , Kempf, B., Kappes, R.M., Bremer, E. 1997. Osmostress response in Bacillus subtilis: characterization of a proline uptake system (OpuE) regulated by high osmolarity and the alternative transcription factor sigma B. Mol. Microbiol. 25:175-187
    • von Blohn, C. von , Kempf, B., Kappes, R.M., Bremer, E. 1997. Osmostress response in Bacillus subtilis: characterization of a proline uptake system (OpuE) regulated by high osmolarity and the alternative transcription factor sigma B. Mol. Microbiol. 25:175-187
  • 87
    • 0035342615 scopus 로고    scopus 로고
    • Sodium-substrate cotransport in bacteria
    • Wilson, T.H., Ding, P.Z. 2001. Sodium-substrate cotransport in bacteria. Biochim. Biophys. Acta. 1505:121-130
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 121-130
    • Wilson, T.H.1    Ding, P.Z.2
  • 88
    • 0033014719 scopus 로고    scopus 로고
    • Osmosensing by bacteria: Signals and membrane-based sensors
    • Wood, J.M. 1999. Osmosensing by bacteria: signals and membrane-based sensors. Microbiol. Mol. Biol. Rev. 63:230-262
    • (1999) Microbiol. Mol. Biol. Rev , vol.63 , pp. 230-262
    • Wood, J.M.1
  • 89
    • 17144398849 scopus 로고    scopus 로고
    • A structural model for the osmosensor, transporter, and osmoregulator ProP of Escherichia coli
    • Wood, J.M., Culham, D.E., Hillar, A., Vernikovska, Y.I., Liu, F., Boggs, J.M., Keates, R.A. 2005. A structural model for the osmosensor, transporter, and osmoregulator ProP of Escherichia coli. Biochemistry 44:5634-5646
    • (2005) Biochemistry , vol.44 , pp. 5634-5646
    • Wood, J.M.1    Culham, D.E.2    Hillar, A.3    Vernikovska, Y.I.4    Liu, F.5    Boggs, J.M.6    Keates, R.A.7
  • 91
    • 0242424106 scopus 로고    scopus 로고
    • Trimeric subunit stoichiometry of the glutamate transporters from Bacillus caldotenax and Bacillus stearothermophilus
    • Yernool, D., Boudker, O., Folta-Stogniew, E., Gouaux, E. 2003. Trimeric subunit stoichiometry of the glutamate transporters from Bacillus caldotenax and Bacillus stearothermophilus. Biochemistry 42:12981-12988
    • (2003) Biochemistry , vol.42 , pp. 12981-12988
    • Yernool, D.1    Boudker, O.2    Folta-Stogniew, E.3    Gouaux, E.4
  • 92
    • 7244254186 scopus 로고    scopus 로고
    • Structure of a glutamate transporter homologue from Pyrococcus horikoshii
    • Yernool, D., Boudker, O., Jin, Y., Gouaux, E. 2004. Structure of a glutamate transporter homologue from Pyrococcus horikoshii. Nature 431:811-818
    • (2004) Nature , vol.431 , pp. 811-818
    • Yernool, D.1    Boudker, O.2    Jin, Y.3    Gouaux, E.4
  • 93
    • 33646445156 scopus 로고    scopus 로고
    • Structure of the multidrug transporter EmrD from Escherichia coli
    • Yin, Y., He, X., Szewczyk, P., Nguyen, T., Chang, G. 2006. Structure of the multidrug transporter EmrD from Escherichia coli. Science 312:741-744
    • (2006) Science , vol.312 , pp. 741-744
    • Yin, Y.1    He, X.2    Szewczyk, P.3    Nguyen, T.4    Chang, G.5
  • 95
    • 0344010237 scopus 로고    scopus 로고
    • Solution structure of the C-terminal antiparallel coiled-coil domain from Escherichia coli osmosensor ProP
    • Zoetewey, D.L., Tripet, B.P., Kutateladze, T.G., Overduin, M.J., Wood, J.M., Hodges, R.S. 2003. Solution structure of the C-terminal antiparallel coiled-coil domain from Escherichia coli osmosensor ProP. J. Mol. Biol. 334:1063-1076
    • (2003) J. Mol. Biol , vol.334 , pp. 1063-1076
    • Zoetewey, D.L.1    Tripet, B.P.2    Kutateladze, T.G.3    Overduin, M.J.4    Wood, J.M.5    Hodges, R.S.6


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