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Volumn 8, Issue 2, 2013, Pages

Recombinant Production of Human Aquaporin-1 to an Exceptional High Membrane Density in Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AQUAPORIN 1; COMPLEMENTARY DNA; ENHANCED GREEN FLUORESCENT PROTEIN; GALACTOSE; RECOMBINANT PROTEIN;

EID: 84873694546     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0056431     Document Type: Article
Times cited : (30)

References (48)
  • 1
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model. Application to complete genomes
    • Krogh A, Larsson B, von Heijne G, Sonnhammer E, (2001) Predicting transmembrane protein topology with a hidden Markov model. Application to complete genomes. J Mol Biol 305: 567-80.
    • (2001) J Mol Biol , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.4
  • 2
    • 71749104018 scopus 로고    scopus 로고
    • Computational analysis of membrane proteins: the largest class of drug targets
    • Arinaminpathy Y, Khurana E, Engelman DM, Gerstein MB, (2009) Computational analysis of membrane proteins: the largest class of drug targets. Drug Discov Today 14: 1130-1135.
    • (2009) Drug Discov Today , vol.14 , pp. 1130-1135
    • Arinaminpathy, Y.1    Khurana, E.2    Engelman, D.M.3    Gerstein, M.B.4
  • 3
    • 36448995359 scopus 로고    scopus 로고
    • High Resolution Crystal Structure of an Engineered Human β2-Adrenergic G protein-Coupled Receptor
    • Cherezov V, Rosenbaum DM, Hanson MA, Rasmussen SGF, Thian FS, et al. (2007) High Resolution Crystal Structure of an Engineered Human β2-Adrenergic G protein-Coupled Receptor. Science 318: 1258-1265.
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1    Rosenbaum, D.M.2    Hanson, M.A.3    Rasmussen, S.G.F.4    Thian, F.S.5
  • 4
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the human β2 adrenergic G-protein-coupled receptor
    • Rasmussen SGF, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, et al. (2007) Crystal structure of the human β2 adrenergic G-protein-coupled receptor. Nature 450: 383-387.
    • (2007) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.F.1    Choi, H.J.2    Rosenbaum, D.M.3    Kobilka, T.S.4    Thian, F.S.5
  • 6
    • 56749103466 scopus 로고    scopus 로고
    • The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist
    • Jaakola VP, Griffith MT, Hanson MA, Cherezov V, Chien EY, et al. (2008) The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322: 1211-7.
    • (2008) Science , vol.322 , pp. 1211-1217
    • Jaakola, V.P.1    Griffith, M.T.2    Hanson, M.A.3    Cherezov, V.4    Chien, E.Y.5
  • 8
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent shaker family K+-channel
    • Long SB, Campbell EB, MacKinnon R, (2006) Crystal structure of a mammalian voltage-dependent shaker family K+-channel. Science 309: 897-903.
    • (2006) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 9
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • Grisshammer C, Tate CG, (1995) Overexpression of integral membrane proteins for structural studies. Q Rev Biophys 28: 315-422.
    • (1995) Q Rev Biophys , vol.28 , pp. 315-422
    • Grisshammer, C.1    Tate, C.G.2
  • 10
    • 32944474055 scopus 로고    scopus 로고
    • Heterologous expression of membrane and soluble proteins derepresses GCN4 mRNA translation in the yeast Saccharomyces cerevisiae
    • Steffensen L, Pedersen PA, (1996) Heterologous expression of membrane and soluble proteins derepresses GCN4 mRNA translation in the yeast Saccharomyces cerevisiae. Eukaryot Cell 5: 248-61.
    • (1996) Eukaryot Cell , vol.5 , pp. 248-261
    • Steffensen, L.1    Pedersen, P.A.2
  • 11
    • 77949488801 scopus 로고    scopus 로고
    • Purification of transmembrane proteins from Saccharomyces cerevisiae for X-ray crystallography
    • Clark KM, Fedoriw N, Robinson K, Connelly SM, Randles J, et al. (2010) Purification of transmembrane proteins from Saccharomyces cerevisiae for X-ray crystallography. Protein Expr Purif 71: 207-23.
    • (2010) Protein Expr Purif , vol.71 , pp. 207-223
    • Clark, K.M.1    Fedoriw, N.2    Robinson, K.3    Connelly, S.M.4    Randles, J.5
  • 12
    • 33645454462 scopus 로고    scopus 로고
    • Optimization of membrane protein over expression and purification using GFP fusions
    • Drew D, Lerch M, Kunji E, Slotboom DJ, de Gier JW, (2006) Optimization of membrane protein over expression and purification using GFP fusions. Nat Methods 3: 303-13.
    • (2006) Nat Methods , vol.3 , pp. 303-313
    • Drew, D.1    Lerch, M.2    Kunji, E.3    Slotboom, D.J.4    de Gier, J.W.5
  • 13
  • 14
    • 79960317704 scopus 로고    scopus 로고
    • Aquaporin at a glance
    • Verkman AS, (2011) Aquaporin at a glance. J Cell Sci 124: 2107-12.
    • (2011) J Cell Sci , vol.124 , pp. 2107-2112
    • Verkman, A.S.1
  • 15
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • Preston GM, Carroll TP, Guggino WB, Agre P, (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256: 385-387.
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 16
    • 0030860531 scopus 로고    scopus 로고
    • Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glyverol and urea
    • Ishibashi K, Kuwahara Y, Gu Y, Kageyama A, Tohsaka A, et al. (1997) Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glyverol and urea. J Biol Chem 272: 20782-20786.
    • (1997) J Biol Chem , vol.272 , pp. 20782-20786
    • Ishibashi, K.1    Kuwahara, Y.2    Gu, Y.3    Kageyama, A.4    Tohsaka, A.5
  • 17
    • 47349127025 scopus 로고    scopus 로고
    • A subgroup of plant aquaporins facilitate the bi-directional diffusion of As(OH)3 and Sb(OH)3 across membranes
    • Bienert GP, Thorsen M, Schussler MD, Nilsson HR, Wagner A, et al. (2008) A subgroup of plant aquaporins facilitate the bi-directional diffusion of As(OH)3 and Sb(OH)3 across membranes. BMC Biol 6: 26.
    • (2008) BMC Biol , vol.6 , pp. 26
    • Bienert, G.P.1    Thorsen, M.2    Schussler, M.D.3    Nilsson, H.R.4    Wagner, A.5
  • 18
    • 33745442045 scopus 로고    scopus 로고
    • The Arabidopsis major intrinsic protein NIP5;1 is essential for efficient boron uptake and plant development under boron limitation
    • Takano J, Wada M Ludewig U, Schaff G, von Wiren N, et al. (2006) The Arabidopsis major intrinsic protein NIP5;1 is essential for efficient boron uptake and plant development under boron limitation. Plant Cell 18: 1498-1509.
    • (2006) Plant Cell , vol.18 , pp. 1498-1509
    • Takano, J.1    Wada, M.2    Ludewig, U.3    Schaff, G.4    von Wiren, N.5
  • 20
    • 0037131175 scopus 로고    scopus 로고
    • Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63
    • Ikeda M, Beitz E, Kozono D, Guggino WB, Agre P, et al. (2002) Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63. J Biol Chem 277: 39873-39879.
    • (2002) J Biol Chem , vol.277 , pp. 39873-39879
    • Ikeda, M.1    Beitz, E.2    Kozono, D.3    Guggino, W.B.4    Agre, P.5
  • 22
    • 33847753534 scopus 로고    scopus 로고
    • Specific aquaporins facilitate the diffusion of hydrogen peroxide across membranes
    • Bienert GP, Møller AL, Kristiansen KA, Schulz A, Møller IM, et al. (2007) Specific aquaporins facilitate the diffusion of hydrogen peroxide across membranes. J Biol Chem 282: 1183-1192.
    • (2007) J Biol Chem , vol.282 , pp. 1183-1192
    • Bienert, G.P.1    Møller, A.L.2    Kristiansen, K.A.3    Schulz, A.4    Møller, I.M.5
  • 23
    • 20644433762 scopus 로고    scopus 로고
    • Reconstituted aquaporin 1 water channels transport CO2 across membranes
    • Prasad GV, Coury LA, Finn F, Zeidel ML, (1998) Reconstituted aquaporin 1 water channels transport CO2 across membranes. J Biol Chem 273: 33123-33126.
    • (1998) J Biol Chem , vol.273 , pp. 33123-33126
    • Prasad, G.V.1    Coury, L.A.2    Finn, F.3    Zeidel, M.L.4
  • 24
    • 33745988574 scopus 로고    scopus 로고
    • Aquaporin-1 transports NO across cell membranes
    • Herrera M, Hong NJ, Garvin JL, (2006) Aquaporin-1 transports NO across cell membranes. Hypertension 48: 157-164.
    • (2006) Hypertension , vol.48 , pp. 157-164
    • Herrera, M.1    Hong, N.J.2    Garvin, J.L.3
  • 25
    • 0032549031 scopus 로고    scopus 로고
    • Severely impaired urinary concentrating ability in transgenic mice lacking aquaporin-1 water channels
    • Ma T, Yang B, Gillespie A, Carlson EJ, Epstein CJ, et al. (1998) Severely impaired urinary concentrating ability in transgenic mice lacking aquaporin-1 water channels. J Biol Chem 273: 4296-4299.
    • (1998) J Biol Chem , vol.273 , pp. 4296-4299
    • Ma, T.1    Yang, B.2    Gillespie, A.3    Carlson, E.J.4    Epstein, C.J.5
  • 26
    • 0035913207 scopus 로고    scopus 로고
    • Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1
    • King LS, Choi M, Fernandez PC, Cartron JP, Agre P, (2001) Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1. N Engl J Med 345: 175-9.
    • (2001) N Engl J Med , vol.345 , pp. 175-179
    • King, L.S.1    Choi, M.2    Fernandez, P.C.3    Cartron, J.P.4    Agre, P.5
  • 27
    • 0027306170 scopus 로고
    • Distribution of the aquaporin CHIP in secretory and resorptive epithelia and capillary endothelia
    • Nielsen S, Smith BL, Christensen EI, Agre P, (1993) Distribution of the aquaporin CHIP in secretory and resorptive epithelia and capillary endothelia. Proc Natl Acad Sci U S A 90: 7275-9.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 7275-7279
    • Nielsen, S.1    Smith, B.L.2    Christensen, E.I.3    Agre, P.4
  • 28
    • 11244254968 scopus 로고    scopus 로고
    • Reduced cerebrospinal fluid production and intracranial pressure in mice lacking choroid plexus water channel Aquaporin-1
    • Oshio K, Watanabe H, Song Y, Verkman AS, Manley GT, (2005) Reduced cerebrospinal fluid production and intracranial pressure in mice lacking choroid plexus water channel Aquaporin-1. FASEB J 19: 76-8.
    • (2005) FASEB J , vol.19 , pp. 76-78
    • Oshio, K.1    Watanabe, H.2    Song, Y.3    Verkman, A.S.4    Manley, G.T.5
  • 29
    • 77958145454 scopus 로고    scopus 로고
    • Aquaporin 1, a potential therapeutic target for migraine with aura
    • Guang-Yin Xu, Fen Wang, Xinghong Jiang, Jin Tao, (2010) Aquaporin 1, a potential therapeutic target for migraine with aura. Molecular pain 6: 68.
    • (2010) Molecular Pain , vol.6 , pp. 68
    • Guang-Yin, X.1    Fen, W.2    Xinghong, J.3    Jin, T.4
  • 30
    • 0035991134 scopus 로고    scopus 로고
    • Renal concentrating and diluting function in deficiency of specific aquaporin genes
    • Verkman AS, (2002) Renal concentrating and diluting function in deficiency of specific aquaporin genes. Exp Nephrol 10: 235-245.
    • (2002) Exp Nephrol , vol.10 , pp. 235-245
    • Verkman, A.S.1
  • 33
    • 0031439976 scopus 로고    scopus 로고
    • Purification and functional reconstitution of the human CHIP28 water channel expressed in Saccharomyces cerevisiae
    • Laizé V, Ripoche P, Tacnet F, (1997) Purification and functional reconstitution of the human CHIP28 water channel expressed in Saccharomyces cerevisiae. Protein Expr Purif 11: 284-288.
    • (1997) Protein Expr Purif , vol.11 , pp. 284-288
    • Laizé, V.1    Ripoche, P.2    Tacnet, F.3
  • 34
    • 0030027897 scopus 로고    scopus 로고
    • Expression in high yield of pig alpha 1 beta 1 Na,K-ATPase and inactive mutants D369N and D807N
    • Pedersen PA, Rasmussen JH, Jorgensen PL, (1996) Expression in high yield of pig alpha 1 beta 1 Na,K-ATPase and inactive mutants D369N and D807N. J Biol Chem 271: 2514-2522.
    • (1996) J Biol Chem , vol.271 , pp. 2514-2522
    • Pedersen, P.A.1    Rasmussen, J.H.2    Jorgensen, P.L.3
  • 35
    • 43149098999 scopus 로고    scopus 로고
    • GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae
    • Drew D, Newstead S, Sonoda Y, Kim H, von Heijne G, et al. (2008) GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae. Nat Protoc 3: 784-98.
    • (2008) Nat Protoc , vol.3 , pp. 784-798
    • Drew, D.1    Newstead, S.2    Sonoda, Y.3    Kim, H.4    von Heijne, G.5
  • 37
    • 0000615498 scopus 로고
    • Plasmid vectors carrying the replication origin of filamentous single stranded phages
    • In: Setlow JK, Hollaender A, eds, New York: Plenum Press
    • Cesareni G, Murray JAH (1987) Plasmid vectors carrying the replication origin of filamentous single stranded phages. In: Setlow JK, Hollaender A, eds. Genetic Engineering, Principles and Methods vol 9.New York: Plenum Press.pp. 135-149.
    • (1987) Genetic Engineering, Principles and Methods , vol.9 , pp. 135-149
    • Cesareni, G.1    Murray, J.A.H.2
  • 38
    • 0035912901 scopus 로고    scopus 로고
    • Role of phylogenetically conserved amino acid residues in folding of Na,K-ATPase
    • Jorgensen JR, Pedersen PA, (2001) Role of phylogenetically conserved amino acid residues in folding of Na,K-ATPase. Biochemistry 40: 7301-08.
    • (2001) Biochemistry , vol.40 , pp. 7301-7308
    • Jorgensen, J.R.1    Pedersen, P.A.2
  • 40
    • 71549146572 scopus 로고    scopus 로고
    • Constructing size distributions of liposomes from single-object fluorescence measurements
    • Lohr C, Kunding AH, Bhaita VK, Stamou D, (2009) Constructing size distributions of liposomes from single-object fluorescence measurements. Method Enzymol vol 465: 143-161.
    • (2009) Method Enzymol , vol.465 , pp. 143-161
    • Lohr, C.1    Kunding, A.H.2    Bhaita, V.K.3    Stamou, D.4
  • 41
    • 0028929242 scopus 로고
    • A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast
    • Vida TA, Emr SD, (1995) A new vital stain for visualizing vacuolar membrane dynamics and endocytosis in yeast. J Cell Biol 128: 775-792.
    • (1995) J Cell Biol , vol.128 , pp. 775-792
    • Vida, T.A.1    Emr, S.D.2
  • 43
    • 33646011258 scopus 로고    scopus 로고
    • Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins
    • Kawate T, Gouaux E, (2006) Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14: 673-681.
    • (2006) Structure , vol.14 , pp. 673-681
    • Kawate, T.1    Gouaux, E.2
  • 44
    • 0021028478 scopus 로고
    • The presence of a defective LEU2 gene on 2 μDNA recombinant plasmids of Saccharomyces cerevisiae is responsible for curing and high copy number
    • Eberhart E, Hollenberg CP, (1983) The presence of a defective LEU2 gene on 2 μDNA recombinant plasmids of Saccharomyces cerevisiae is responsible for curing and high copy number. J Bacteriol 156: 625-635.
    • (1983) J Bacteriol , vol.156 , pp. 625-635
    • Eberhart, E.1    Hollenberg, C.P.2
  • 45
    • 84855989800 scopus 로고    scopus 로고
    • Production of the stable human histamine H1 receptor in Pichia pastoris for structural determination
    • Shiroishi M, Kobayashi T, Ogasawara S, Tsujimoto H, Ikeda-Suno C, et al. (2011) Production of the stable human histamine H1 receptor in Pichia pastoris for structural determination. Methods 55: 281-286.
    • (2011) Methods , vol.55 , pp. 281-286
    • Shiroishi, M.1    Kobayashi, T.2    Ogasawara, S.3    Tsujimoto, H.4    Ikeda-Suno, C.5
  • 46
    • 35348832935 scopus 로고    scopus 로고
    • High-throughput fluorescent based optimization of eukaryotic membrane protein overexpression and purification in Saccharomyces cerevisiae
    • Newstead S, Kim H, von Heijne G, Iwata S, Drew D, (2007) High-throughput fluorescent based optimization of eukaryotic membrane protein overexpression and purification in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 104: 13936-13941.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 13936-13941
    • Newstead, S.1    Kim, H.2    von Heijne, G.3    Iwata, S.4    Drew, D.5
  • 47
  • 48


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