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EmrE, a model for studying evolution and mechanism of ion-coupled transporters

Schuldiner, Shimon·2009·Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
DOI 10.1016/j.bbapap.2008.12.018
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Abstract

EmrE is a small (110 residues) SMR transporter from Escherichia coli that extrudes positively charged aromatic drugs in exchange for two protons, thus rendering bacteria resistant to a variety of toxic compounds. Due to its size, stability and retention of its function upon solubilization in detergent, EmrE provides a unique experimental paradigm for the biochemical and biophysical studies of membrane based ion-coupled transporters. In addition, EmrE has been in center stage in the past two years because it provides also a paradigm for the study of the evolution of membrane proteins. Controversy around this topic is still going on and some novel concepts are surfacing that may contribute to our understanding of evolution of topology of membrane proteins. Furthermore, based on the findings that the cell multidrug transporters interact functionally we introduce the concept of a cell Resistosome.

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Research works printed but not linked: 124

  1. Nikaido, 1998, Multiple antibiotic resistance and efflux, Curr. Opin. Microbiol., 1, 516, 10.1016/S1369-5274(98)80083-0 · DOI
  2. Paulsen, 1996, Proton-dependent multidrug efflux systems, Microbiol. Rev., 60, 575, 10.1128/MMBR.60.4.575-608.1996 · DOI
  3. Saier, 1998, Evolutionary origins of multidrug and drug-specific efflux pumps in bacteria, FASEB J., 12, 265, 10.1096/fasebj.12.3.265 · DOI
  4. Schuldiner, 2001, Precious things come in little packages, J. Mol. Microbiol. Biotechnol., 3, 155
  5. Schuldiner, 2001, Small is mighty: EmrE, a multidrug transporter as an experimental paradigm, News Physiol. Sci., 16, 130
  6. Yerushalmi, 2000, A model for coupling of H(+) and substrate fluxes based on “time-sharing” of a common binding site, Biochemistry, 39, 14711, 10.1021/bi001892i · DOI
  7. Yerushalmi, 2000, A common binding site for substrates and protons in EmrE, an ion-coupled multidrug transporter, FEBS Lett., 476, 93, 10.1016/S0014-5793(00)01677-X · DOI
  8. Schuldiner, 1997, EmrE, the smallest ion-coupled transporter, provides a unique paradigm for structure-function studies, J. Exp. Biol., 200, 335, 10.1242/jeb.200.2.335 · DOI
  9. Yerushalmi, 1995, EmrE, an Escherichia coli 12-kDa multidrug transporter, exchanges toxic cations and H+ and is soluble in organic solvents, J. Biol. Chem., 270, 6856, 10.1074/jbc.270.12.6856 · DOI
  10. Soskine, 2004, Direct evidence for substrate induced proton release in detergent solubilized EmrE, a multidrug transporter, J. Biol. Chem., 279, 9951, 10.1074/jbc.M312853200 · DOI
  11. Schuldiner, 2007, When biochemistry meets structural biology: the cautionary tale of EmrE, Trends Biochem.Sci., 32, 252, 10.1016/j.tibs.2007.04.002 · DOI
  12. Adam, 2007, The fast release of sticky protons: Kinetics of substrate binding and proton release in a multidrug transporter, Proc. Natl. Acad. Sci. U. S. A., 104, 17989, 10.1073/pnas.0704425104 · DOI
  13. Schuldiner, 2007, Controversy over EmrE structure, Science, 317, 748, 10.1126/science.317.5839.748d · DOI
  14. Rapp, 2007, Emulating membrane protein evolution by rational design, Science, 315, 1282, 10.1126/science.1135406 · DOI
  15. Steiner-Mordoch, 2008, Parallel topology of genetically fused EmrE homodimers, EMBO J., 27, 17, 10.1038/sj.emboj.7601951 · DOI
  16. Purewal, 1991, Nucleotide sequence of the ethidium efflux gene from Escherichia coli, FEMS Microbiol. Lett., 82, 229, 10.1111/j.1574-6968.1991.tb04870.x · DOI
  17. Morimyo, 1992, Cloning and characterization of the mvrC gene of Escherichia coli K12 which confers resistance against methyl viologen toxicity, Nucleic Acids Res., 20, 3159, 10.1093/nar/20.12.3159 · DOI
  18. Midgley, 1987, An efflux system for cationic dyes and related compounds in Escherichia coli, Microbiol. Sci., 4, 125
  19. Grinius, 1992, A staphylococcal multidrug resistance gene product is a member of a new protein family, Plasmid, 27, 119, 10.1016/0147-619X(92)90012-Y · DOI
  20. Grinius, 1994, Bacterial multidrug resistance is due to a single membrane protein which functions as a drug pump, J. Biol. Chem., 269, 29998, 10.1016/S0021-9258(18)43980-4 · DOI
  21. Paulsen, 1996, The SMR family: a novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs, Mol. Microbiol., 19, 1167, 10.1111/j.1365-2958.1996.tb02462.x · DOI
  22. Bay, 2008, Small multidrug resistance proteins: a multidrug transporter family that continues to grow, Biochim. Biophys. Acta, 1778, 1814, 10.1016/j.bbamem.2007.08.015 · DOI
  23. Ninio, 2003, Characterization of an archaeal multidrug transporter with a unique amino acid composition, J. Biol. Chem., 278, 12000, 10.1074/jbc.M213119200 · DOI
  24. Ninio, 2001, Functional analysis of novel multidrug transporters from human pathogens, J. Biol. Chem., 276, 48250, 10.1074/jbc.M108231200 · DOI
  25. Jack, 2000, A broad-specificity multidrug efflux pump requiring a pair of homologous SMR-type proteins, J. Bacteriol., 182, 2311, 10.1128/JB.182.8.2311-2313.2000 · DOI
  26. Dobrindt, 2002, Genetic structure and distribution of four pathogenicity islands (PAI I(536) to PAI IV(536)) of uropathogenic Escherichia coli strain 536, Infect. Immun., 70, 6365, 10.1128/IAI.70.11.6365-6372.2002 · DOI
  27. Chen, 2006, Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach, Proc. Natl. Acad. Sci. U. S. A., 103, 5977, 10.1073/pnas.0600938103 · DOI
  28. Chung, 2001, SMR-type multidrug resistance pumps, Curr. Opin. Drug Discov. Dev., 4, 237
  29. Neyfakh, 2002, Mystery of multidrug transporters: the answer can be simple, Mol. Microbiol., 44, 1123, 10.1046/j.1365-2958.2002.02965.x · DOI
  30. Neyfakh, 1997, Natural functions of bacterial multidrug transporters, Trends Microbiol., 5, 309, 10.1016/S0966-842X(97)01064-0 · DOI
  31. Krulwich, 2005, Do physiological roles foster persistence of drug/multidrug-efflux transporters? A case study, Nat. Rev., 3, 566, 10.1038/nrmicro1181 · DOI
  32. Sulavik, 2001, Antibiotic susceptibility profiles of Escherichia coli strains lacking multidrug efflux pump genes, Antimicrob. Agents Chemother., 45, 1126, 10.1128/AAC.45.4.1126-1136.2001 · DOI
  33. Nishino, 2001, Analysis of a complete library of putative drug transporter genes in Escherichia coli, J. Bacteriol., 183, 5803, 10.1128/JB.183.20.5803-5812.2001 · DOI
  34. Lee, 2000, Interplay between efflux pumps may provide either additive or multiplicative effects on drug resistance, J. Bacteriol., 182, 3142, 10.1128/JB.182.11.3142-3150.2000 · DOI
  35. Yang, 2003, Relative contributions of the AcrAB, MdfA and NorE efflux pumps to quinolone resistance in Escherichia coli, J. Antimicrob. Chemother., 51, 545, 10.1093/jac/dkg126 · DOI
  36. Yerushalmi, 2000, An essential glutamyl residue in EmrE, a multidrug antiporter from Escherichia coli, J. Biol. Chem., 275, 5264, 10.1074/jbc.275.8.5264 · DOI
  37. Yerushalmi, 2001, A single carboxyl mutant of the multidrug transporter EmrE is fully functional, J. Biol. Chem., 276, 12744, 10.1074/jbc.M010979200 · DOI
  38. Gutman, 2003, An amino acid cluster around the essential Glu-14 is part of the substrate and proton binding domain of EmrE, a multidrug transporter from Escherichia coli, J. Biol. Chem., 278, 16082, 10.1074/jbc.M213120200 · DOI
  39. Weinglass, 2005, Exploring the role of a unique carboxyl residue in EmrE by mass spectrometry, J. Biol. Chem., 280, 7487, 10.1074/jbc.M413555200 · DOI
  40. Sharoni, 2005, Exploring the binding domain of EmrE, the smallest multidrug transporter, J. Biol. Chem., 280, 32849, 10.1074/jbc.M504910200 · DOI
  41. Muth, 2000, A membrane-embedded glutamate is required for ligand binding to the multidrug transporter EmrE, EMBO J., 19, 234, 10.1093/emboj/19.2.234 · DOI
  42. Rotem, 2004, EmrE, a multidrug transporter from Escherichia coli, transports monovalent and divalent substrates with the same stoichiometry, J. Biol. Chem., 279, 48787, 10.1074/jbc.M408187200 · DOI
  43. Ninio, 2004, The membrane topology of EmrE – a small multidrug transporter from Escherichia coli, FEBS Lett., 562, 193, 10.1016/S0014-5793(04)00240-6 · DOI
  44. Koteiche, 2003, Structure of the substrate binding pocket of the multidrug transporter EmrE: site-directed spin labeling of transmembrane segment 1, Biochemistry, 42, 6099, 10.1021/bi0342867 · DOI
  45. Elbaz, 2005, Substrate-induced tryptophan fluorescence changes in emre, the smallest ion-coupled multidrug transporter, Biochemistry, 44, 7369, 10.1021/bi050356t · DOI
  46. Rotem, 2006, Identification of tyrosine residues critical for the function of an ion-coupled multidrug transporter, J. Biol. Chem., 281, 18715, 10.1074/jbc.M602088200 · DOI
  47. Zheleznova, 2000, A structure-based mechanism for drug binding by multidrug transporters, Trends Biochem. Sci., 25, 39, 10.1016/S0968-0004(99)01514-5 · DOI
  48. Murray, 2004, Crystal structures of QacR-diamidine complexes reveal additional multidrug-binding modes and a novel mechanism of drug charge neutralization, J. Biol. Chem., 279, 14365, 10.1074/jbc.M313870200 · DOI
  49. Seeger, 2006, Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism, Science, 313, 1295, 10.1126/science.1131542 · DOI
  50. Murakami, 2006, Crystal structures of a multidrug transporter reveal a functionally rotating mechanism, Nature, 443, 173, 10.1038/nature05076 · DOI
  51. Dougherty, 1996, Cation–pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp, Science, 271, 163, 10.1126/science.271.5246.163 · DOI
  52. Elbaz, 2008, Identification of a glycine motif required for packing in EmrE, a multidrug transporter from Escherichia coli, J. Biol. Chem., 283, 12276, 10.1074/jbc.M710338200 · DOI
  53. Jiang, 2002, The open pore conformation of potassium channels, Nature, 417, 523, 10.1038/417523a · DOI
  54. Weinglass, 2001, Engineering conformational flexibility in the lactose permease of Escherichia coli: use of glycine-scanning mutagenesis to rescue mutant Glu325-->Asp, Biochemistry, 40, 769, 10.1021/bi002171m · DOI
  55. Senes, 2000, Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with beta-branched residues at neighboring positions, J. Mol. Biol., 296, 921, 10.1006/jmbi.1999.3488 · DOI
  56. Liu, 2002, Genomic analysis of membrane protein families: abundance and conserved motifs, Genome Biol., 3, 10.1186/gb-2002-3-10-research0054 · DOI
  57. Zhou, 2005, Transporter-associated currents in the gamma-aminobutyric acid transporter GAT-1 are conditionally impaired by mutations of a conserved glycine residue, J. Biol. Chem., 280, 20316, 10.1074/jbc.M412937200 · DOI
  58. Han, 1997, The C9 methyl group of retinal interacts with glycine-121 in rhodopsin, Proc. Natl. Acad. Sci. U. S. A., 94, 13442, 10.1073/pnas.94.25.13442 · DOI
  59. Han, 1996, The effects of amino acid replacements of glycine 121 on transmembrane helix 3 of rhodopsin, J. Biol. Chem., 271, 32330, 10.1074/jbc.271.50.32330 · DOI
  60. Soskine, 2006, On parallel and antiparallel topology of an homodimeric multidrug transporter, J. Biol. Chem., 281, 36205, 10.1074/jbc.M607186200 · DOI
  61. Gottschalk, 2004, A structural model of EmrE, a multi-drug transporter from Escherichia coli, Biophys. J., 86, 3335, 10.1529/biophysj.103.034546 · DOI
  62. Soskine, 2002, Crosslinking of membrane-embedded cysteines reveals contact points in the EmrE oligomer, Proc. Natl. Acad. Sci. U. S. A., 99, 12043, 10.1073/pnas.192392899 · DOI
  63. Schwaiger, 1998, NMR investigation of the multidrug transporter EmrE, an integral membrane protein, Eur. J. Biochem., 254, 610, 10.1046/j.1432-1327.1998.2540610.x · DOI
  64. Arkin, 1996, Determining the secondary structure and orientation of EmrE, a multi-drug transporter, indicates a transmembrane four-helix bundle, Biochemistry, 35, 7233, 10.1021/bi960094i · DOI
  65. Butler, 2004, The Escherichia coli multidrug transporter EmrE is a dimer in the detergent-solubilised state., J. Mol. Biol., 340, 797, 10.1016/j.jmb.2004.05.014 · DOI
  66. Ubarretxena-Belandia, 2003, Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer, EMBO J., 22, 6175, 10.1093/emboj/cdg611 · DOI · Paper page
  67. Tate, 2001, The projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 A resolution, EMBO J., 20, 77, 10.1093/emboj/20.1.77 · DOI
  68. Elbaz, 2004, In vitro synthesis of fully functional EmrE, a multidrug transporter, and study of its oligomeric state, Proc. Natl. Acad. Sci. U. S. A., 101, 1519, 10.1073/pnas.0306533101 · DOI
  69. Tate, 2003, Conformational changes in the multidrug transporter EmrE associated with substrate binding, J. Mol. Biol., 332, 229, 10.1016/S0022-2836(03)00895-7 · DOI
  70. Rotem, 2001, In vitro monomer swapping in EmrE, a multidrug transporter from Escherichia coli, reveals that the oligomer is the functional unit, J. Biol. Chem., 276, 48243, 10.1074/jbc.M108229200 · DOI
  71. Yerushalmi, 1996, Negative dominance studies demonstrate the oligomeric structure of emre, a multidrug antiporter from Escherichia coli, J. Biol. Chem., 271, 31044, 10.1074/jbc.271.49.31044 · DOI
  72. Paulsen, 1995, Molecular characterization of the staphylococcal multidrug resistance export protein QacC, J. Bacteriol., 177, 2827, 10.1128/jb.177.10.2827-2833.1995 · DOI
  73. Li, 2003, Contributions of MexAB-OprM and an EmrE homolog to intrinsic resistance of Pseudomonas aeruginosa to aminoglycosides and dyes, Antimicrob. Agents Chemother., 47, 27, 10.1128/AAC.47.1.27-33.2003 · DOI
  74. Masaoka, 2000, A two-component multidrug efflux pump, EbrAB, in Bacillus subtilis, J. Bacteriol., 182, 2307, 10.1128/JB.182.8.2307-2310.2000 · DOI
  75. Ganas, 2007, A two-component small multidrug resistance pump functions as a metabolic valve during nicotine catabolism by Arthrobacter nicotinovorans, Microbiology, 153, 1546, 10.1099/mic.0.2006/004234-0 · DOI
  76. Rapp, 2006, Identification and evolution of dual-topology membrane proteins, Nat. Struct. Mol. Biol., 13, 112, 10.1038/nsmb1057 · DOI
  77. Zhang, 2007, Functional characterization of the heterooligomeric EbrAB multidrug efflux transporter of Bacillus subtilis, Biochemistry, 46, 5218, 10.1021/bi7001604 · DOI
  78. Kikukawa, 2007, Anti-parallel membrane topology of two components of EbrAB, a multidrug transporter, Biochem. Biophys. Res. Commun., 358, 1071, 10.1016/j.bbrc.2007.05.032 · DOI
  79. Kikukawa, 2006, Two-component bacterial multidrug transporter, EbrAB: mutations making each component solely functional, Biochim. Biophys. Acta, 1758, 673, 10.1016/j.bbamem.2006.04.004 · DOI
  80. Geertsma, 2005, Functional interactions between the subunits of the lactose transporter from Streptococcus thermophilus, J. Mol. Biol., 350, 102, 10.1016/j.jmb.2005.04.047 · DOI
  81. Yernool, 2004, Structure of a glutamate transporter homologue from Pyrococcus horikoshii, Nature, 431, 811, 10.1038/nature03018 · DOI
  82. Veenhoff, 2002, Quaternary structure and function of transport proteins, Trends Biochem. Sci., 27, 242, 10.1016/S0968-0004(02)02077-7 · DOI
  83. Lanyi, 2004, Bacteriorhodopsin, Ann Rev. Physiol., 66, 665, 10.1146/annurev.physiol.66.032102.150049 · DOI
  84. Williams, 1999, Projection structure of NhaA, a secondary transporter from Escherichia coli, at 4.0 A resolution, EMBO J., 18, 3558, 10.1093/emboj/18.13.3558 · DOI
  85. Y. Fujiyoshi, K. Mitsuoka, B.L. de Groot, A. Philippsen, H. Grubmüller, P. Agre, A. Engel, Structure and Function of Water Channels, Current Opinion in Structural Biology 12 (2002) 509–515. · DOI
  86. Klingenberg, 1981, Membrane protein oligomeric structure and transport function, Nature, 290, 449, 10.1038/290449a0 · DOI
  87. Pebay-Peyroula, 2004, Nucleotide exchange in mitochondria: insight at a molecular level, Curr. Opin. Struct. Biol., 14, 420, 10.1016/j.sbi.2004.06.009 · DOI
  88. Bamber, 2007, The yeast mitochondrial ADP/ATP carrier functions as a monomer in mitochondrial membranes, Proc. Natl. Acad. Sci. U. S. A., 104, 10830, 10.1073/pnas.0703969104 · DOI
  89. Lehner, 2008, The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric, J. Biol. Chem., 283, 3281, 10.1074/jbc.M707899200 · DOI
  90. Ma, 2004, Structure of the multidrug resistance efflux transporter EmrE from Escherichia coli, Proc. Natl. Acad. Sci. U. S. A., 101, 2852, 10.1073/pnas.0400137101 · DOI
  91. Pornillos, 2005, X-ray structure of the EmrE multidrug transporter in complex with a substrate, Science, 310, 1950, 10.1126/science.1119776 · DOI
  92. Fleishman, 2006, Quasi-symmetry in the cryo-EM structure of EmrE provides the key to modeling its transmembrane domain, J. Mol. Biol., 364, 54, 10.1016/j.jmb.2006.08.072 · DOI
  93. Tate, 2006, Comparison of three structures of the multidrug transporter EmrE, Curr. Opin. Struct. Biol., 16, 457, 10.1016/j.sbi.2006.06.005 · DOI
  94. Fleishman, 2006, Progress in structure prediction of alpha-helical membrane proteins, Curr. Opin. Struct. Biol., 16, 496, 10.1016/j.sbi.2006.06.003 · DOI
  95. Chang, 2006, Retraction, Science, 314, 1875, 10.1126/science.314.5807.1875b · DOI
  96. Murata, 2000, Structural determinants of water permeation through aquaporin-1, Nature, 407, 599, 10.1038/35036519 · DOI
  97. Dutzler, 2002, X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity, Nature, 415, 287, 10.1038/415287a · DOI · Paper page
  98. Yamashita, 2005, Crystal structure of a bacterial homologue of Na+/Cl-dependent neurotransmitter transporters, Nature, 437, 215, 10.1038/nature03978 · DOI
  99. Chen, 2007, X-ray structure of EmrE supports dual topology model, Proc. Natl. Acad. Sci. U. S. A., 104, 18999, 10.1073/pnas.0709387104 · DOI
  100. Green, 2001, Quantitative evaluation of the lengths of homobifunctional protein cross-linking reagents used as molecular rulers, Protein Sci., 10, 1293, 10.1110/ps.51201 · DOI
  101. Poolman, 2007, Biochemistry. A missing link in membrane protein evolution, Science, 315, 1229, 10.1126/science.1140073 · DOI
  102. Daley, 2005, Global topology analysis of the Escherichia coli inner membrane proteome, Science, 308, 1321, 10.1126/science.1109730 · DOI
  103. Manoil, 1986, A genetic approach to analyzing membrane protein topology, Science, 233, 1403, 10.1126/science.3529391 · DOI
  104. Feilmeier, 2000, Green fluorescent protein functions as a reporter for protein localization in Escherichia coli, J. Bacteriol., 182, 4068, 10.1128/JB.182.14.4068-4076.2000 · DOI
  105. McHaourab, 2008, Role of sequence bias in the topology of the multidrug transporter EmrE, Biochemistry, 47, 7980, 10.1021/bi800628d · DOI
  106. Uebel, 1997, Recognition principle of the TAP transporter disclosed by combinatorial peptide libraries, Proc. Natl. Acad. Sci., 94, 8976, 10.1073/pnas.94.17.8976 · DOI
  107. Murakami, 2008, Multidrug efflux transporter, AcrB–the pumping mechanism, Curr. Opin. Struct. Biol., 18, 459, 10.1016/j.sbi.2008.06.007 · DOI
  108. Schuldiner, 1995, Vesicular neurotransmitter transporters: from bacteria to humans, Physiol. Rev., 75, 369, 10.1152/physrev.1995.75.2.369 · DOI
  109. Yelin, 1995, The pharmacological profile of the vesicular monoamine transporter resembles that of multidrug transporters, FEBS Lett., 377, 201, 10.1016/0014-5793(95)01346-6 · DOI
  110. Bravo, 2005, New transport assay demonstrates vesicular acetylcholine transporter has many alternative substrates, Neurochem. Int., 47, 243, 10.1016/j.neuint.2005.05.002 · DOI
  111. Girvin, 1995, Determination of local protein structure by spin label difference 2D NMR: the region neighboring Asp61 of Subunit c of the F1F0 ATP synthase, Biochemistry, 34, 1635, 10.1021/bi00005a020 · DOI
  112. Girvin, 1993, Helical structure and folding of subunit c of F1Fo ATP synthase, Biochemistry, 32, 12167, 10.1021/bi00096a029 · DOI
  113. Orekhov, 1994, Backbone dynamics of (1–71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy, Eur. J. Biochem., 219, 887, 10.1111/j.1432-1033.1994.tb18570.x · DOI
  114. Sikora, 2005, Investigation of ligand binding to the multidrug resistance protein EmrE by isothermal titration calorimetry, Biophys. J., 88, 475, 10.1529/biophysj.104.049247 · DOI
  115. Molteni, 2001, Identification of a small-molecule binding site at the dimer interface of the HIV integrase catalytic domain, Acta Crystallogr., D Biol. Crystallogr., 57, 536, 10.1107/S0907444901001652 · DOI
  116. Lolkema, 1983, The transmembrane electrical potential in Rhodopseudomonas sphaeroides determined from the distribution of tetraphenylphosphonium after correction for its binding to cell components, Eur. J. Biochem., 130, 287, 10.1111/j.1432-1033.1983.tb07149.x · DOI
  117. Betton, 2003, Rapid translation system (RTS): a promising alternative for recombinant protein production, Curr. Protein Pept. Sci., 4, 73, 10.2174/1389203033380359 · DOI
  118. Zubay, 1973, In vitro synthesis of protein in microbial systems, Annu. Rev. Genet., 7, 267, 10.1146/annurev.ge.07.120173.001411 · DOI
  119. Sawasaki, 2002, A cell-free protein synthesis system for high-throughput proteomics, Proc. Natl. Acad. Sci. U. S. A., 99, 14652, 10.1073/pnas.232580399 · DOI
  120. Morita, 2003, A wheat germ cell-free system is a novel way to screen protein folding and function, Protein Sci., 12, 1216, 10.1110/ps.0241203 · DOI
  121. Doi, 2002, Novel fluorescence labeling and high-throughput assay technologies for in vitro analysis of protein interactions, Genome Res., 12, 487, 10.1101/gr.218802. Article published online before print in February 2002 · DOI
  122. Zhang, 1996, Sequence requirements for membrane assembly of polytopic membrane proteins: molecular dissection of the membrane insertion process and topogenesis of the human MDR3 P-glycoprotein, Mol. Biol. Cell, 7, 1709, 10.1091/mbc.7.11.1709 · DOI
  123. Heinrich, 2003, Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane, EMBO J., 22, 3654, 10.1093/emboj/cdg346 · DOI
  124. Nagamori, 2003, In vitro synthesis of lactose permease to probe the mechanism of membrane insertion and folding, J. Biol. Chem., 278, 14820, 10.1074/jbc.M300332200 · DOI

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Metadata

Authors
Schuldiner, S.
Venue
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Publisher
Elsevier BV
Published
2009-05
Volume
1794
Issue
5
Pages
748-762
ISSN
1570-9639
DOI
10.1016/j.bbapap.2008.12.018
Cited by
164
References
1
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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Schuldiner, S. (2009). EmrE, a model for studying evolution and mechanism of ion-coupled transporters. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. https://doi.org/10.1016/j.bbapap.2008.12.018