메뉴 건너뛰기




Volumn 37, Issue 2, 2000, Pages 254-262

The Escherichia coli aquaporin-Z water channel

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN; BACTERIAL PROTEIN; WATER;

EID: 0033913601     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2000.02016.x     Document Type: Review
Times cited : (97)

References (38)
  • 1
    • 0032510966 scopus 로고    scopus 로고
    • The aquaporins, blueprints for cellular plumbing systems
    • Agre, P., Bonhivers, M., and Borgnia, M. (1998) The aquaporins, blueprints for cellular plumbing systems. J Biol Chem 273: 14659-14662.
    • (1998) J Biol Chem , vol.273 , pp. 14659-14662
    • Agre, P.1    Bonhivers, M.2    Borgnia, M.3
  • 2
    • 0029883930 scopus 로고    scopus 로고
    • Structure of Aquaporin-2 vasopressin water channel
    • Bai, L., Fushimi, K., Sasaki, S., and Marumo, F. (1996) Structure of Aquaporin-2 vasopressin water channel. J Biol Chem 271: 5171-5176.
    • (1996) J Biol Chem , vol.271 , pp. 5171-5176
    • Bai, L.1    Fushimi, K.2    Sasaki, S.3    Marumo, F.4
  • 4
    • 0033118214 scopus 로고    scopus 로고
    • Managing hypoosmotic stress: Aquaporins and mechanosensitive channels in Escherichia coli
    • Booth, I.R., and Louis, P. (1999) Managing hypoosmotic stress: aquaporins and mechanosensitive channels in Escherichia coli. Curr Opin Microbiol 2: 166-169.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 166-169
    • Booth, I.R.1    Louis, P.2
  • 5
    • 0033520342 scopus 로고    scopus 로고
    • Functional reconstitution and characterization of AqpZ, the E. coli water channel protein
    • Borgnia, M.J., Kozono, D., Calamita, G., Maloney, P.C., and Agre, P. (1999) Functional reconstitution and characterization of AqpZ, the E. coli water channel protein. J Mol Biol 291: 1169-1179.
    • (1999) J Mol Biol , vol.291 , pp. 1169-1179
    • Borgnia, M.J.1    Kozono, D.2    Calamita, G.3    Maloney, P.C.4    Agre, P.5
  • 6
    • 0033619938 scopus 로고    scopus 로고
    • Oligomerization state of MIP proteins expressed in Xenopus oocytes as revealed by freeze-fracture electron-microscopy analysis
    • Bron, P., Lagree, V., Froger, A., Rolland, J.P., Hubert, J.F., Delamarche, C., et al. (1999) Oligomerization state of MIP proteins expressed in Xenopus oocytes as revealed by freeze-fracture electron-microscopy analysis. J Struct Biol 128: 287-296.
    • (1999) J Struct Biol , vol.128 , pp. 287-296
    • Bron, P.1    Lagree, V.2    Froger, A.3    Rolland, J.P.4    Hubert, J.F.5    Delamarche, C.6
  • 7
    • 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., and Agre, P. (1995) Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli. J Biol Chem 270: 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
    • 0031443814 scopus 로고    scopus 로고
    • The Aquaporin-Z water channel gene of Escherichia coli: Structure, organization and phylogeny
    • Calamita, G., Kempf, B., Rudd, K.E., Bonhivers, M., Kneip, S., Bishai, W.R., et al. (1997) The Aquaporin-Z water channel gene of Escherichia coli: structure, organization and phylogeny. Biol Cell 89: 321-329.
    • (1997) Biol Cell , vol.89 , pp. 321-329
    • Calamita, G.1    Kempf, B.2    Rudd, K.E.3    Bonhivers, M.4    Kneip, S.5    Bishai, W.R.6
  • 10
    • 0034125522 scopus 로고    scopus 로고
    • The complete DNA sequence of the O antigen gene region of Plesiomonas shigelloides serotype 017 which is identical to Shigella sonnei form I antigen
    • Chida, T., Okamura, N., Ohtani, K., Yoshida, Y., Arakawa, E., and Watanabe, H. (2000) The complete DNA sequence of the O antigen gene region of Plesiomonas shigelloides serotype 017 which is identical to Shigella sonnei form I antigen. Microbiol Immunol 44: 161-172.
    • (2000) Microbiol Immunol , vol.44 , pp. 161-172
    • Chida, T.1    Okamura, N.2    Ohtani, K.3    Yoshida, Y.4    Arakawa, E.5    Watanabe, H.6
  • 11
    • 0026006215 scopus 로고
    • Prokaryotic osmoregulation: Genetics and physiology
    • Csonka, L.N., and Hanson, A.D. (1991) Prokaryotic osmoregulation: genetics and physiology. Annu Rev Microbiol 45: 569-606.
    • (1991) Annu Rev Microbiol , vol.45 , pp. 569-606
    • Csonka, L.N.1    Hanson, A.D.2
  • 12
    • 0032788791 scopus 로고    scopus 로고
    • Visualization of AqpZ-mediated water permeability in Escherichia coli by cryoelectron microscopy
    • Delamarche, C., Thomas, D., Rolland, J.-P., Froger, A., Gouranton, J., Svelto, M., et al. (1999) Visualization of AqpZ-mediated water permeability in Escherichia coli by cryoelectron microscopy. J Bacteriol 181: 4193-4197.
    • (1999) J Bacteriol , vol.181 , pp. 4193-4197
    • Delamarche, C.1    Thomas, D.2    Rolland, J.-P.3    Froger, A.4    Gouranton, J.5    Svelto, M.6
  • 13
    • 0034161393 scopus 로고    scopus 로고
    • The importance of aquaporin water channel protein structures
    • Engel, A., Fujiyoshi, Y., and Agre, P. (2000) The importance of aquaporin water channel protein structures. EMBO J 19: 800-806.
    • (2000) EMBO J , vol.19 , pp. 800-806
    • Engel, A.1    Fujiyoshi, Y.2    Agre, P.3
  • 14
    • 0030807170 scopus 로고    scopus 로고
    • The wacA gene of Dictyostelium discoideum is a developmentally regulated member of the MIP family
    • Flick, K.M., Shaulsky, G., and Loomis, W.F. (1997) The wacA gene of Dictyostelium discoideum is a developmentally regulated member of the MIP family. Gene 195: 127-130.
    • (1997) Gene , vol.195 , pp. 127-130
    • Flick, K.M.1    Shaulsky, G.2    Loomis, W.F.3
  • 15
    • 0028371413 scopus 로고
    • Nucleotide sequence and expression of a ripening and water stress-related cDNA from tomato with homology to the MIP class of membrane channel protein
    • Fray, R.G., Wallace, A., Grierson, D., and Lycett, G.W. (1994) Nucleotide sequence and expression of a ripening and water stress-related cDNA from tomato with homology to the MIP class of membrane channel protein. Plant Mol Biol 24: 539-543.
    • (1994) Plant Mol Biol , vol.24 , pp. 539-543
    • Fray, R.G.1    Wallace, A.2    Grierson, D.3    Lycett, G.W.4
  • 16
    • 0031777369 scopus 로고    scopus 로고
    • Prediction of functional residues in water channels and related proteins
    • Froger, A., Tallur, B., Thomas, D., and Delamarche, C. (1998) Prediction of functional residues in water channels and related proteins. Protein Sci 7: 1458-1468.
    • (1998) Protein Sci , vol.7 , pp. 1458-1468
    • Froger, A.1    Tallur, B.2    Thomas, D.3    Delamarche, C.4
  • 17
    • 0030915821 scopus 로고    scopus 로고
    • Isolation of a gene encoding nodulin-like intrinsic protein of Escherichia coli
    • Fushimi, K., Bai, L., Marumo, F., and Sasaki, S. (1997) Isolation of a gene encoding nodulin-like intrinsic protein of Escherichia coli. Biochem Mol Biol Int 41: 995-1003.
    • (1997) Biochem Mol Biol Int , vol.41 , pp. 995-1003
    • Fushimi, K.1    Bai, L.2    Marumo, F.3    Sasaki, S.4
  • 19
    • 0031786140 scopus 로고    scopus 로고
    • Genetic analysis of Shigella sonnei form I antigen: Identification of a novel IS630 as an essential element for the form I antigen expression
    • Houng, H.S., and Venkatesan, M.M. (1998) Genetic analysis of Shigella sonnei form I antigen: identification of a novel IS630 as an essential element for the form I antigen expression. Microb Pathog 25: 165-173.
    • (1998) Microb Pathog , vol.25 , pp. 165-173
    • Houng, H.S.1    Venkatesan, M.M.2
  • 21
    • 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., and Agre, P. (1994) Molecular structure of the water channel through aquaporin-CHIP. The hourglass model. J Biol Chem 269: 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
  • 22
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko, T., Sato, S., Kotani, H., Tanaka, A., Asamizu, E., Nakamura, Y., et al. (1996) Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res 3: 109-136.
    • (1996) DNA Res , vol.3 , pp. 109-136
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Tanaka, A.4    Asamizu, E.5    Nakamura, Y.6
  • 23
    • 0029148735 scopus 로고
    • A Synechococcus gene encoding a putative pore-forming intrinsic membrane protein
    • Kashiwagi, S., Kanamaru, K., and Mizuno, T. (1995) A Synechococcus gene encoding a putative pore-forming intrinsic membrane protein. Biochim Biophys Acta 1237: 189-192.
    • (1995) Biochim Biophys Acta , vol.1237 , pp. 189-192
    • Kashiwagi, S.1    Kanamaru, K.2    Mizuno, T.3
  • 24
    • 0008537747 scopus 로고    scopus 로고
    • Microbial water and glycerol channels
    • Agre, P., Nielsen, S., and Hohmann, S. (eds). Academic Press (in press)
    • Kayingo, G., Bill, R., Calamita, G., Hohmann, S., and Prior, B.A. (2000) Microbial water and glycerol channels. In Aquaporins. Agre, P., Nielsen, S., and Hohmann, S. (eds). Academic Press (in press).
    • (2000) Aquaporins
    • Kayingo, G.1    Bill, R.2    Calamita, G.3    Hohmann, S.4    Prior, B.A.5
  • 25
    • 0003036460 scopus 로고
    • 2O through living membranes. Effect of neurohypophyseal hormone on isolated anuran skin
    • 2O through living membranes. Effect of neurohypophyseal hormone on isolated anuran skin. Acta Physiol Scand 28: 60-76.
    • (1953) Acta Physiol Scand , vol.28 , pp. 60-76
    • Koefoed-Johnsen, V.1    Ussing, H.H.2
  • 26
    • 0033927503 scopus 로고    scopus 로고
    • Polymorphism of Saccharomyces cerevisiae aquaporins
    • in press
    • Laizé, V., Tacnet, F., Ripoche, P., and Hohmann, S. (2000) Polymorphism of Saccharomyces cerevisiae aquaporins. Yeast (in press).
    • (2000) Yeast
    • Laizé, V.1    Tacnet, F.2    Ripoche, P.3    Hohmann, S.4
  • 28
    • 0032484119 scopus 로고    scopus 로고
    • Bidirectional water fluxes and specificity for small hydrophobic molecules in Aquaporin 0-5
    • Meinild, A.K., Klaerke, D.A., and Zeuthen, T. (1998) Bidirectional water fluxes and specificity for small hydrophobic molecules in Aquaporin 0-5. J Biol Chem 273: 32446-32451.
    • (1998) J Biol Chem , vol.273 , pp. 32446-32451
    • Meinild, A.K.1    Klaerke, D.A.2    Zeuthen, T.3
  • 29
    • 0027144124 scopus 로고
    • Cellular and subcellular immunolocalization of vasopressin-regulated water channel in rat kidney
    • Nielsen, S., DiGiovanni, S.R., Christensen, E.I., Knepper, M.A., and Harris, H.W. (1993) Cellular and subcellular immunolocalization of vasopressin-regulated water channel in rat kidney. Proc Natl Acad Sci USA 90: 11663-11667.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11663-11667
    • Nielsen, S.1    DiGiovanni, S.R.2    Christensen, E.I.3    Knepper, M.A.4    Harris, H.W.5
  • 30
    • 0029910115 scopus 로고    scopus 로고
    • Phylogenetic characterization of the MIP family of transmembrane channel proteins
    • Park, J.H., and Saier, H.M., Jr (1996) Phylogenetic characterization of the MIP family of transmembrane channel proteins. J Membr Biol 153: 171-180.
    • (1996) J Membr Biol , vol.153 , pp. 171-180
    • Park, J.H.1    Saier H.M., Jr.2
  • 31
    • 0031875675 scopus 로고    scopus 로고
    • Regulation of compatible solute accumulation in bacteria
    • Poolman, B., and Glaasker, E. (1998) Regulation of compatible solute accumulation in bacteria. Mol Microbiol 29: 397-407.
    • (1998) Mol Microbiol , vol.29 , pp. 397-407
    • Poolman, B.1    Glaasker, E.2
  • 32
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 water channel
    • Preston, G.M., Piazza-Carroll, P., Guggino, W.B., and Agre, P. (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 water channel. Science 256: 385-387.
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Piazza-Carroll, P.2    Guggino, W.B.3    Agre, P.4
  • 33
    • 0033520347 scopus 로고    scopus 로고
    • Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography
    • Ringler, P., Borgnia, M.J., Stahlberg, H., Maloney, P.C., Agre, P., and Engel, A. (1999) Structure of the water channel AqpZ from Escherichia coli revealed by electron crystallography. J Mol Biol 291: 1181-1190.
    • (1999) J Mol Biol , vol.291 , pp. 1181-1190
    • Ringler, P.1    Borgnia, M.J.2    Stahlberg, H.3    Maloney, P.C.4    Agre, P.5    Engel, A.6
  • 34
    • 0030953720 scopus 로고    scopus 로고
    • Antimonite is accumulated by the glycerol facilitator GIpF in Escherichia coli
    • Sanders, O.I., Rensing, C., Kuroda, M., Mitra, B., and Rosen, B. (1997) Antimonite is accumulated by the glycerol facilitator GIpF in Escherichia coli. J Bacteriol 179: 3365-3367.
    • (1997) J Bacteriol , vol.179 , pp. 3365-3367
    • Sanders, O.I.1    Rensing, C.2    Kuroda, M.3    Mitra, B.4    Rosen, B.5
  • 35
    • 0033568641 scopus 로고    scopus 로고
    • High resolution AFM topographs of the Escherichia coli water channel Aquaporin-Z
    • Scheuring, S., Ringler, P., Borgnia, M.J., Stahlberg, H., Müller, D.J., Agre, P., et al. (1999) High resolution AFM topographs of the Escherichia coli water channel Aquaporin-Z. EMBO J 18: 4981-4987.
    • (1999) EMBO J , vol.18 , pp. 4981-4987
    • Scheuring, S.1    Ringler, P.2    Borgnia, M.J.3    Stahlberg, H.4    Müller, D.J.5    Agre, P.6
  • 36
    • 0343484957 scopus 로고    scopus 로고
    • Pulsed high-field gradient in vivo NMR spectroscopy to measure diffusional water permeability in Corynebacterium glutamicum
    • Schobert, S.M., Bar, N.K., Kramer, R., and Karger, J. (2000) Pulsed high-field gradient in vivo NMR spectroscopy to measure diffusional water permeability in Corynebacterium glutamicum. Anal Biochem 279: 100-105.
    • (2000) Anal Biochem , vol.279 , pp. 100-105
    • Schobert, S.M.1    Bar, N.K.2    Kramer, R.3    Karger, J.4
  • 38
    • 0033547240 scopus 로고    scopus 로고
    • Rapid gating and anion permeability of an intracellular aquaporin
    • Yasui, M., Hazama, A., Kwon, T.H., Nielsen, S., Guggino, W.B., and Agre, P. (1999) Rapid gating and anion permeability of an intracellular aquaporin. Nature 402: 184-187.
    • (1999) Nature , vol.402 , pp. 184-187
    • Yasui, M.1    Hazama, A.2    Kwon, T.H.3    Nielsen, S.4    Guggino, W.B.5    Agre, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.