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Volumn 291, Issue 5, 1999, Pages 1169-1179

Functional reconstitution and characterization of AqpZ, the E. coli water channel protein

Author keywords

Aquaporin; Bacterial; Channel structure; Gene family; Water transport

Indexed keywords

AQUAPORIN; GLYCEROL; HISTIDINE; SORBITOL; UREA;

EID: 0033520342     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3032     Document Type: Article
Times cited : (259)

References (35)
  • 1
    • 0028335265 scopus 로고
    • Sequence and functional expression of an amphibian water channel, FA-CHIP: A new member of the MIP family
    • Abrami L., Simon M., Rousselet G., Berthonaud V., Buhler J. M., Ripoche P. Sequence and functional expression of an amphibian water channel, FA-CHIP: a new member of the MIP family. Biochim. Biophys. Acta. 1192:1994;147-151.
    • (1994) Biochim. Biophys. Acta , vol.1192 , pp. 147-151
    • Abrami, L.1    Simon, M.2    Rousselet, G.3    Berthonaud, V.4    Buhler, J.M.5    Ripoche, P.6
  • 2
    • 0022827885 scopus 로고
    • Bacterial anion exchange. Use of osmolytes during solubilization and reconstitution of phosphate-linked antiport fromStreptococcus lactis
    • Ambudkar S. V., Maloney P. C. Bacterial anion exchange. Use of osmolytes during solubilization and reconstitution of phosphate-linked antiport fromStreptococcus lactis. J. Biol. Chem. 261:1986;10079-10086.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10079-10086
    • Ambudkar, S.V.1    Maloney, P.C.2
  • 4
    • 0032538552 scopus 로고    scopus 로고
    • Aquaporins in Saccharomyces. Genetic and functional distinctions between laboratory and wild-type strains
    • Bonhivers M., Carbrey J. M., Gould S. J., Agre P. Aquaporins in Saccharomyces. Genetic and functional distinctions between laboratory and wild-type strains. J. Biol. Chem. 273:1998;27565-27572.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27565-27572
    • Bonhivers, M.1    Carbrey, J.M.2    Gould, S.J.3    Agre, P.4
  • 5
    • 0028787084 scopus 로고
    • Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli
    • Calamita G., Bishai W. R., Preston G. M., Guggino W. B., Agre P. Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli. J. Biol. Chem. 270:1995;29063-29066.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29063-29066
    • Calamita, G.1    Bishai, W.R.2    Preston, G.M.3    Guggino, W.B.4    Agre, P.5
  • 8
    • 0031890395 scopus 로고    scopus 로고
    • Reconstitution of water channel function of aquaporins 1 and 2 by expression in yeast secretory vesicles
    • Coury L. A., Mathai J. C., Prasad G. V., Brodsky J. L., Agre P., Zeidel M. L. Reconstitution of water channel function of aquaporins 1 and 2 by expression in yeast secretory vesicles. Am. J. Physiol. 274:1998;F34-F42.
    • (1998) Am. J. Physiol. , vol.274
    • Coury, L.A.1    Mathai, J.C.2    Prasad, G.V.3    Brodsky, J.L.4    Agre, P.5    Zeidel, M.L.6
  • 11
    • 0016657917 scopus 로고
    • Solubilization of membranes by detergents
    • Helenius A., Simons K. Solubilization of membranes by detergents. Biochim. Biophys. Acta. 415:1975;29-79.
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 12
    • 0032562998 scopus 로고    scopus 로고
    • 2+ion links the cytoplasmic tail of CD4 and the N-terminal region of Lck
    • 2+ion links the cytoplasmic tail of CD4 and the N-terminal region of Lck. J. Biol. Chem. 273:1998;18729-18733.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18729-18733
    • Huse, M.1    Eck, M.J.2    Harrison, S.C.3
  • 13
    • 0028318868 scopus 로고
    • Molecular structure of the water channel through aquaporin CHIP. The hourglass model
    • Jung J. S., Preston G. M., Smith B. L., Guggino W. B., Agre P. Molecular structure of the water channel through aquaporin CHIP. The hourglass model. J. Biol. Chem. 269:1994;14648-14654.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14648-14654
    • Jung, J.S.1    Preston, G.M.2    Smith, B.L.3    Guggino, W.B.4    Agre, P.5
  • 14
    • 0032524648 scopus 로고    scopus 로고
    • A yeast recombinant aquaporin mutant that is not expressed or mistargeted in Xenopus oocyte can be functionally analyzed in reconstituted proteoliposomes
    • Lagree V., Pellerin I., Hubert J. F., Tacnet F., Le Caherec F., Roudier N., Thomas D., Gouranton J., Deschamps S. A yeast recombinant aquaporin mutant that is not expressed or mistargeted in Xenopus oocyte can be functionally analyzed in reconstituted proteoliposomes. J. Biol. Chem. 273:1998;12422-12426.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12422-12426
    • Lagree, V.1    Pellerin, I.2    Hubert, J.F.3    Tacnet, F.4    Le, C.F.5    Roudier, N.6    Thomas, D.7    Gouranton, J.8    Deschamps, S.9
  • 17
    • 0030915303 scopus 로고    scopus 로고
    • Molecular design of aquaporin-1 water channel as revealed by electron crystallography
    • Li H., Lee S., Jap B. K. Molecular design of aquaporin-1 water channel as revealed by electron crystallography. Nature Struct. Biol. 4:1997;263-265.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 263-265
    • Li, H.1    Lee, S.2    Jap, B.K.3
  • 18
    • 0029852885 scopus 로고    scopus 로고
    • CDNA cloning of a functional water channel from toad urinary bladder epithelium
    • Ma T., Yang B., Verkman A. S. cDNA cloning of a functional water channel from toad urinary bladder epithelium. Am. J. Physiol. 271:1996;C1699-C1704.
    • (1996) Am. J. Physiol. , vol.271
    • Ma, T.1    Yang, B.2    Verkman, A.S.3
  • 19
    • 0033579812 scopus 로고    scopus 로고
    • Hourglass pore-forming domains restrict aquaporin-1 tetramer assembly
    • Mathai J. C., Agre P. Hourglass pore-forming domains restrict aquaporin-1 tetramer assembly. Biochemistry. 38:1999;923-928.
    • (1999) Biochemistry , vol.38 , pp. 923-928
    • Mathai, J.C.1    Agre, P.2
  • 20
    • 0029910115 scopus 로고    scopus 로고
    • Phylogenetic characterization of the MIP family of transmembrane channel proteins
    • Park J. H., Saier M. H. Phylogenetic characterization of the MIP family of transmembrane channel proteins. J. Membr. Biol. 153:1996;171-180.
    • (1996) J. Membr. Biol. , vol.153 , pp. 171-180
    • Park, J.H.1    Saier, M.H.2
  • 21
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • Preston G. M., Carroll T. P., Guggino W. B., Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science. 256:1992;385-387.
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 22
    • 0027472168 scopus 로고
    • The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel
    • Preston G. M., Jung J. S., Guggino W. B., Agre P. The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel. J. Biol. Chem. 268:1993;17-20.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17-20
    • Preston, G.M.1    Jung, J.S.2    Guggino, W.B.3    Agre, P.4
  • 23
    • 0033520347 scopus 로고    scopus 로고
    • Structure of water channel Aqpz from Escherichia coli revealed by electron crystallography
    • Ringler P., Borgnia M. J., Stahlberg H., Maloney P., Agre P., Engel A. Structure of water channel Aqpz from Escherichia coli revealed by electron crystallography. J. Mol. Biol. 291:1999;1181-1190.
    • (1999) J. Mol. Biol. , vol.291 , pp. 1181-1190
    • Ringler, P.1    Borgnia, M.J.2    Stahlberg, H.3    Maloney, P.4    Agre, P.5    Engel, A.6
  • 24
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner W., Weissmann C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56:1973;502-514.
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 25
    • 0025922827 scopus 로고
    • r28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins
    • r28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. J. Biol. Chem. 266:1991;6407-6415.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6407-6415
    • Smith, B.L.1    Agre, P.2
  • 26
    • 0031194164 scopus 로고    scopus 로고
    • Purification of UhpT, the sugar phosphate transporter of Escherichia coli
    • Tamai E., Fann M. C., Tsuchiya T., Maloney P. C. Purification of UhpT, the sugar phosphate transporter of Escherichia coli. Protein Exp. Purif. 10:1997;275-282.
    • (1997) Protein Exp. Purif. , vol.10 , pp. 275-282
    • Tamai, E.1    Fann, M.C.2    Tsuchiya, T.3    Maloney, P.C.4
  • 27
    • 0026639874 scopus 로고
    • Functional reconstitution of the isolated erythrocyte water channel CHIP28
    • van Hoek A. N., Verkman A. S. Functional reconstitution of the isolated erythrocyte water channel CHIP28. J. Biol. Chem. 267:1992;18267-18269.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18267-18269
    • Van Hoek, A.N.1    Verkman, A.S.2
  • 29
    • 0028275784 scopus 로고
    • The three-dimensional structure of human erythrocyte aquaporin CHIP
    • Walz T., Smith B. L., Agre P., Engel A. The three-dimensional structure of human erythrocyte aquaporin CHIP. EMBO J. 13:1994;2985-2993.
    • (1994) EMBO J. , vol.13 , pp. 2985-2993
    • Walz, T.1    Smith, B.L.2    Agre, P.3    Engel, A.4
  • 31
    • 0031200862 scopus 로고    scopus 로고
    • The major intrinsic protein family of Arabidopsis has 23 members that form three distinct groups with functional aquaporins in each group
    • Weig A., Deswarte C., Chrispeels M. J. The major intrinsic protein family of Arabidopsis has 23 members that form three distinct groups with functional aquaporins in each group. Pl. Physiol. 114:1997;1347-1357.
    • (1997) Pl. Physiol. , vol.114 , pp. 1347-1357
    • Weig, A.1    Deswarte, C.2    Chrispeels, M.J.3
  • 32
    • 0030922070 scopus 로고    scopus 로고
    • Water and glycerol permeabilities of aquaporins 1-5 and MIP determined quantitatively by expression of epitope-tagged constructs in Xenopus oocytes
    • Yang B., Verkman A. S. Water and glycerol permeabilities of aquaporins 1-5 and MIP determined quantitatively by expression of epitope-tagged constructs in Xenopus oocytes. J. Biol. Chem. 272:1997;16140-16146.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16140-16146
    • Yang, B.1    Verkman, A.S.2
  • 33
    • 0026806764 scopus 로고
    • Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
    • Zeidel M. L., Ambudkar S. V., Smith B. L., Agre P. Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein. Biochemistry. 31:1992;7436-7440.
    • (1992) Biochemistry , vol.31 , pp. 7436-7440
    • Zeidel, M.L.1    Ambudkar, S.V.2    Smith, B.L.3    Agre, P.4
  • 34
    • 0028314729 scopus 로고
    • Ultrastructure, pharmacologic inhibition, and transport selectivity of aquaporin channel-forming integral protein in proteoliposomes
    • Zeidel M. L., Nielsen S., Smith B. L., Ambudkar S. V., Maunsbach A. B., Agre P. Ultrastructure, pharmacologic inhibition, and transport selectivity of aquaporin channel-forming integral protein in proteoliposomes. Biochemistry. 33:1994;1606-1615.
    • (1994) Biochemistry , vol.33 , pp. 1606-1615
    • Zeidel, M.L.1    Nielsen, S.2    Smith, B.L.3    Ambudkar, S.V.4    Maunsbach, A.B.5    Agre, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.