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Volumn 150, Issue 8, 1999, Pages 507-520

Membrane topology of CadA homologous P-type ATPase of Helicobacter pylori as determined by expression of phoA fusions in Escherichia coli and the positive inside rule

Author keywords

ATPase; CadA; Cytoplasmic membrane; Helicobacter pylori; phoA; Positive inside rule; Topology

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALKALINE PHOSPHATASE; BACTERIAL ENZYME; DNA FRAGMENT; HYBRID PROTEIN;

EID: 0032714260     PISSN: 09232508     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0923-2508(99)00106-0     Document Type: Article
Times cited : (25)

References (44)
  • 2
    • 0028098714 scopus 로고
    • Membrane topology of multidrug resistance protein expressed in Escherichia coli. N-terminal domain
    • Bibi E., Beja O. Membrane topology of multidrug resistance protein expressed in Escherichia coli. N-terminal domain. J. Biol. Chem. 269:1994;19910-19915.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19910-19915
    • Bibi, E.1    Beja, O.2
  • 3
    • 0027509460 scopus 로고
    • Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions
    • Boyd D., Traxler B., Beckwith J. Analysis of the topology of a membrane protein by using a minimum number of alkaline phosphatase fusions. J. Bacteriol. 175:1993;553-556.
    • (1993) J. Bacteriol. , vol.175 , pp. 553-556
    • Boyd, D.1    Traxler, B.2    Beckwith, J.3
  • 4
    • 0031842580 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, and expression of a chemoreceptor gene from Leptospirillum ferroxidans
    • Delgado M., Toledo H., Jerez C.A. Molecular cloning, sequencing, and expression of a chemoreceptor gene from Leptospirillum ferroxidans. Appl. Environ. Microbiol. 64:1998;2380-2385.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2380-2385
    • Delgado, M.1    Toledo, H.2    Jerez, C.A.3
  • 5
    • 0025836761 scopus 로고
    • Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm
    • Derman A.I., Beckwith J. Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm. J. Bacteriol. 173:1991;7719-7722.
    • (1991) J. Bacteriol. , vol.173 , pp. 7719-7722
    • Derman, A.I.1    Beckwith, J.2
  • 6
    • 0027457077 scopus 로고
    • A signal sequence is not required for protein export in prlA mutants of Escherichia coli
    • Derman A.I., Puziss J.W., Bassford P.J., Beckwith J. A signal sequence is not required for protein export in prlA mutants of Escherichia coli. EMBO J. 12:1993;879-888.
    • (1993) EMBO J. , vol.12 , pp. 879-888
    • Derman, A.I.1    Puziss, J.W.2    Bassford, P.J.3    Beckwith, J.4
  • 8
    • 0025052350 scopus 로고
    • Genetic analysis of membrane protein topology by a sandwich gene fusion approach
    • Ehrmann M., Boyd D., Beckwith J. Genetic analysis of membrane protein topology by a sandwich gene fusion approach. Proc. Natl. Acad. Sci. USA. 87:1990;7574-7578.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7574-7578
    • Ehrmann, M.1    Boyd, D.2    Beckwith, J.3
  • 9
    • 0028986792 scopus 로고
    • Nucleotide sequence and mutational analysis indicate that two Helicobacter pylori genes encode a P-type ATPase and a cation-binding protein associated with copper transport
    • Ge Z., Hiratsuka K., Taylor D. Nucleotide sequence and mutational analysis indicate that two Helicobacter pylori genes encode a P-type ATPase and a cation-binding protein associated with copper transport. Mol. Microbiol. 15:1995;97-106.
    • (1995) Mol. Microbiol. , vol.15 , pp. 97-106
    • Ge, Z.1    Hiratsuka, K.2    Taylor, D.3
  • 10
    • 0011179980 scopus 로고
    • A plasmid facilitating in vitro construction of phoA gene fusions in Escherichia coli
    • Gutierrez C., Devedjian J. A plasmid facilitating in vitro construction of phoA gene fusions in Escherichia coli. Nucleic Acids Res. 17:1989;3999.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 3999
    • Gutierrez, C.1    Devedjian, J.2
  • 11
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman L.M., Belin D., Carson M., Beckwith J. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177:1995;4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.3    Beckwith, J.4
  • 12
    • 0029144920 scopus 로고
    • Probing the transmembrane topology of cyclic nucleotide-gated ion channels with a gene fusion approach
    • Henn D., Baumann A., Kaupp U. Probing the transmembrane topology of cyclic nucleotide-gated ion channels with a gene fusion approach. Proc. Natl. Acad. Sci. USA. 92:1995;7425-7429.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7425-7429
    • Henn, D.1    Baumann, A.2    Kaupp, U.3
  • 13
    • 0032791578 scopus 로고    scopus 로고
    • The Helicobacter pylori CadA gene encodes an essential Cd, Zn, and Co resistance determinant influencing urease activity
    • Herrmann L., Schwan D., Garner R., Mobley H.L.T., Haas R., Schäfer K.P., Melchers K. The Helicobacter pylori CadA gene encodes an essential Cd, Zn, and Co resistance determinant influencing urease activity. Mol. Microbiol. 33:1999;524-536.
    • (1999) Mol. Microbiol. , vol.33 , pp. 524-536
    • Herrmann, L.1    Schwan, D.2    Garner, R.3    Mobley, H.L.T.4    Haas, R.5    Schäfer, K.P.6    Melchers, K.7
  • 14
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 15
    • 0028116716 scopus 로고
    • Topological analysis of the human beta 2-adrenergic receptor expressed in Escherichia coli
    • Lacatena R., Cellini A., Scavizzi F., Tocchini-Valentini G. Topological analysis of the human beta 2-adrenergic receptor expressed in Escherichia coli. Proc. Natl. Acad. Sci. USA. 91:1994;10521-10525.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10521-10525
    • Lacatena, R.1    Cellini, A.2    Scavizzi, F.3    Tocchini-Valentini, G.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0023691364 scopus 로고
    • Isolation of a spiral-shaped bacterium from the cat stomach
    • Lee A., Hazell S., O'Rourke J., Kouprach S. Isolation of a spiral-shaped bacterium from the cat stomach. Infect. Immun. 56:1988;2843-2850.
    • (1988) Infect. Immun. , vol.56 , pp. 2843-2850
    • Lee, A.1    Hazell, S.2    O'Rourke, J.3    Kouprach, S.4
  • 18
    • 0028866670 scopus 로고
    • Organization of P-Type ATPases: Significance of structural diversity
    • Lutsenko S., Kaplan J.H. Organization of P-Type ATPases: significance of structural diversity. Biochemistry. 34:1995;15607-15613.
    • (1995) Biochemistry , vol.34 , pp. 15607-15613
    • Lutsenko, S.1    Kaplan, J.H.2
  • 19
    • 0000632797 scopus 로고
    • TnphoA: A transposon probe for protein export signals
    • Manoil C., Beckwith J. TnphoA: a transposon probe for protein export signals. Proc. Natl. Acad. Sci. USA. 82:1985;8129-8133.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8129-8133
    • Manoil, C.1    Beckwith, J.2
  • 20
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil C., Beckwith J. A genetic approach to analyzing membrane protein topology. Science. 233:1986;1403-1408.
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 21
    • 0029916337 scopus 로고    scopus 로고
    • Capacity of Helicobacter pylori to generate ionic gradients at low pH is similar to that of bacteria which grow under strongly acidic conditions
    • Matin A., Zychlinsky E., Keyhan M., Sachs G. Capacity of Helicobacter pylori to generate ionic gradients at low pH is similar to that of bacteria which grow under strongly acidic conditions. Infect. Immun. 64:1996;1434-1436.
    • (1996) Infect. Immun. , vol.64 , pp. 1434-1436
    • Matin, A.1    Zychlinsky, E.2    Keyhan, M.3    Sachs, G.4
  • 24
    • 0029815909 scopus 로고    scopus 로고
    • The effect of environmental pH on the proton motive force of Helicobacter pylori
    • Meyer-Rosberg K., Scott D.R., Rex D., Melchers K., Sachs G. The effect of environmental pH on the proton motive force of Helicobacter pylori. Gastroenterology. 111:1996;886-900.
    • (1996) Gastroenterology , vol.111 , pp. 886-900
    • Meyer-Rosberg, K.1    Scott, D.R.2    Rex, D.3    Melchers, K.4    Sachs, G.5
  • 25
    • 0020581487 scopus 로고
    • Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli
    • Michaelis S., Inouye H., Oliver D., Beckwith J. Mutations that alter the signal sequence of alkaline phosphatase in Escherichia coli. J. Bacteriol. 154:1983;366-374.
    • (1983) J. Bacteriol. , vol.154 , pp. 366-374
    • Michaelis, S.1    Inouye, H.2    Oliver, D.3    Beckwith, J.4
  • 26
  • 27
    • 0028930318 scopus 로고
    • Helicobacter pylori nickel-transport gene nixA: Synthesis of catalytically active urease in Escherichia coli independent of growth conditions
    • Mobley H., Garner R., Bauerfeind P. Helicobacter pylori nickel-transport gene nixA: synthesis of catalytically active urease in Escherichia coli independent of growth conditions. Mol. Microbiol. 16:1995;97-109.
    • (1995) Mol. Microbiol. , vol.16 , pp. 97-109
    • Mobley, H.1    Garner, R.2    Bauerfeind, P.3
  • 29
    • 0029879233 scopus 로고    scopus 로고
    • The role of Helicobacter pylori urease in the pathogenesis of gastritis and peptic ulceration
    • Mobley H., T L. The role of Helicobacter pylori urease in the pathogenesis of gastritis and peptic ulceration. Aliment. Pharmacol. Ther. 10:1996;57-64.
    • (1996) Aliment. Pharmacol. Ther. , vol.10 , pp. 57-64
    • Mobley, H.1    T., L.2
  • 30
    • 0032478813 scopus 로고    scopus 로고
    • The protein translocation apparatus contributes to determining the topology of an integral membrane protein in Escherichia coli
    • Prinz W., Boyd D., Ehrmann M., Beckwith J. The protein translocation apparatus contributes to determining the topology of an integral membrane protein in Escherichia coli. J. Biol. Chem. 273:1998;8419-8424.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8419-8424
    • Prinz, W.1    Boyd, D.2    Ehrmann, M.3    Beckwith, J.4
  • 31
    • 0031658740 scopus 로고    scopus 로고
    • Influence of pH on metabolism and urease activity of Helicobacter pylori
    • Rektorschek M., Weeks D., Sachs G., Melchers K. Influence of pH on metabolism and urease activity of Helicobacter pylori. Gastroenterology. 115:1998;628-641.
    • (1998) Gastroenterology , vol.115 , pp. 628-641
    • Rektorschek, M.1    Weeks, D.2    Sachs, G.3    Melchers, K.4
  • 34
    • 0029792315 scopus 로고    scopus 로고
    • Bacterial heavy metal rsistance: New surprises
    • Silver S., Phung L. Bacterial heavy metal rsistance: new surprises. Ann. Rev. Microbiol. 50:1996;753-789.
    • (1996) Ann. Rev. Microbiol. , vol.50 , pp. 753-789
    • Silver, S.1    Phung, L.2
  • 35
    • 0027444708 scopus 로고
    • Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium
    • Smith D., Tao T., Maguire M. Membrane topology of a P-type ATPase. The MgtB magnesium transport protein of Salmonella typhimurium. J. Biol. Chem. 268:1993;22469-22479.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22469-22479
    • Smith, D.1    Tao, T.2    Maguire, M.3
  • 36
    • 0030199612 scopus 로고    scopus 로고
    • CPx-type ATPases: A class of P-type ATPases that pump heavy metals
    • Solioz M., Vulpe C. CPx-type ATPases: a class of P-type ATPases that pump heavy metals. Trends Biochem. Sci. 21:1996;237-241.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 237-241
    • Solioz, M.1    Vulpe, C.2
  • 38
    • 0027478779 scopus 로고
    • The topological analysis of integral membrane proteins
    • Traxler B., Boyd D., Beckwith J. The topological analysis of integral membrane proteins. J. Membrane Biol. 132:1993;1-11.
    • (1993) J. Membrane Biol. , vol.132 , pp. 1-11
    • Traxler, B.1    Boyd, D.2    Beckwith, J.3
  • 39
    • 0028111572 scopus 로고
    • Requirements for translocation of periplasmic domains in polytopic membrane proteins
    • Uhland K., Ehrle R., Zander T., Ehrmann M. Requirements for translocation of periplasmic domains in polytopic membrane proteins. J. Bacteriol. 176:1994;4565-4571.
    • (1994) J. Bacteriol. , vol.176 , pp. 4565-4571
    • Uhland, K.1    Ehrle, R.2    Zander, T.3    Ehrmann, M.4
  • 41
    • 0032076479 scopus 로고    scopus 로고
    • Bioenergetics and cytoplasmic membrane stability of the extremely acidophilic, thermophilic archaeon Picrophilus oshimae
    • van deVossenberg J., Driessen A., Zillig W., Konings W. Bioenergetics and cytoplasmic membrane stability of the extremely acidophilic, thermophilic archaeon Picrophilus oshimae. Extremophiles. 2:1998;67-74.
    • (1998) Extremophiles , vol.2 , pp. 67-74
    • Van Devossenberg, J.1    Driessen, A.2    Zillig, W.3    Konings, W.4
  • 42
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacteria inner membrane proteins correlates with the trans-membrane topology
    • vonHeijne G. The distribution of positively charged residues in bacteria inner membrane proteins correlates with the trans-membrane topology. EMBO J. 5:1986;3021-3027.
    • (1986) EMBO J. , vol.5 , pp. 3021-3027
    • Vonheijne, G.1
  • 43
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E., vonHeijne G. Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci. 7:1998;1029-1038.
    • (1998) Protein Sci. , vol.7 , pp. 1029-1038
    • Wallin, E.1    Vonheijne, G.2
  • 44
    • 0032560170 scopus 로고    scopus 로고
    • Structure of the calcium pump from sarcoplasmic reticulum at 8-A resolution
    • Zhang P., Toyoshima C., Yonekura K., Green N., Stokes D. Structure of the calcium pump from sarcoplasmic reticulum at 8-A resolution. Nature. 392:1998;835-839.
    • (1998) Nature , vol.392 , pp. 835-839
    • Zhang, P.1    Toyoshima, C.2    Yonekura, K.3    Green, N.4    Stokes, D.5


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