메뉴 건너뛰기




Volumn 24, Issue 3, 1998, Pages 133-143

Identification of iron-regulated proteins of Mycobacterium tuberculosis and cloning of tandem genes encoding a low iron-induced protein and a metal transporting ATPase with similarities to two-component metal transport systems

Author keywords

ATPase; Iron; Metal transport; Mycobacterium tuberculosis

Indexed keywords

ADENOSINE TRIPHOSPHATASE;

EID: 0031932979     PISSN: 08824010     EISSN: None     Source Type: Journal    
DOI: 10.1006/mpat.1997.9999     Document Type: Article
Times cited : (32)

References (39)
  • 1
    • 0028127357 scopus 로고
    • Identification of genes involved in the sequestration of iron in mycobacteria: The ferric exochelin biosynthetic and uptake pathways
    • Fiss EH, Yu S, Jacobs WR. Identification of genes involved in the sequestration of iron in mycobacteria: the ferric exochelin biosynthetic and uptake pathways. Mol Micro 1994; 14: 557-569.
    • (1994) Mol Micro , vol.14 , pp. 557-569
    • Fiss, E.H.1    Yu, S.2    Jacobs, W.R.3
  • 2
    • 0002444291 scopus 로고
    • Iron metabolism in Mycobacterium
    • Winkelmann D, van der Helm D, Neilands JB, Eds. Weinheim, VCH Verlagsgesellshaft
    • Ratledge C. Iron metabolism in Mycobacterium. In: Winkelmann D, van der Helm D, Neilands JB, Eds. Iron Transport in Microbes, Plants, and Animals. Weinheim, VCH Verlagsgesellshaft, 1987: 207-221.
    • (1987) Iron Transport in Microbes, Plants, and Animals , pp. 207-221
    • Ratledge, C.1
  • 3
    • 0029913805 scopus 로고    scopus 로고
    • Exochelins of Mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the M. tuberculosis cell wall
    • Gobin J, Horwitz MA. Exochelins of Mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the M. tuberculosis cell wall. J Exp Med 1996; 183: 1527-1532.
    • (1996) J Exp Med , vol.183 , pp. 1527-1532
    • Gobin, J.1    Horwitz, M.A.2
  • 4
    • 0028999977 scopus 로고
    • Iron acquisition by Mycobacterium tuberculosis: Isolation and characterization of a family of iron-binding exochelins
    • Gobin J, Moore CH, Reeve Jr JR, Wong DK, Gibson BW, Horwitz MA. Iron acquisition by Mycobacterium tuberculosis: Isolation and characterization of a family of iron-binding exochelins. Proc Natl Acad Sci USA 1995; 92: 5189-5193.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5189-5193
    • Gobin, J.1    Moore, C.H.2    Reeve J.R., Jr.3    Wong, D.K.4    Gibson, B.W.5    Horwitz, M.A.6
  • 6
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam R, Saier Jr MH. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol Rev 1993; 57: 320-346.
    • (1993) Microbiol Rev , vol.57 , pp. 320-346
    • Tam, R.1    Saier M.H., Jr.2
  • 8
    • 0026642657 scopus 로고
    • Characterization of the major membrane protein of virulent Mycobacterium tuberculosis
    • Lee B-Yu, Hefta SA, Brennan PJ. Characterization of the major membrane protein of virulent Mycobacterium tuberculosis. Infect Immun 1992; 60: 2066-2074.
    • (1992) Infect Immun , vol.60 , pp. 2066-2074
    • Lee, B.-Yu.1    Hefta, S.A.2    Brennan, P.J.3
  • 9
    • 0028921689 scopus 로고
    • Analysis of the Mycobacterium tuberculosis 85A Antigen Promoter Region
    • Kremer L, Baulard A, Estaquier J, Content J, Capron A, Locht C. Analysis of the Mycobacterium tuberculosis 85A Antigen Promoter Region. J Bact 1995; 177: 642-653.
    • (1995) J Bact , vol.177 , pp. 642-653
    • Kremer, L.1    Baulard, A.2    Estaquier, J.3    Content, J.4    Capron, A.5    Locht, C.6
  • 10
    • 0028866670 scopus 로고
    • Organization of P-type ATPases: Significance of structural diversity
    • Lutsenko S, Kaplan JH. Organization of P-type ATPases: significance of structural diversity. Biochem (ACS) 1995; 34: 15607-15613.
    • (1995) Biochem (ACS) , vol.34 , pp. 15607-15613
    • Lutsenko, S.1    Kaplan, J.H.2
  • 11
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Møller JC, Juul B, le Maire M. Structural organization, ion transport, and energy transduction of P-type ATPases. Biochem et Biophys Acta 1996; 1286: 1-51.
    • (1996) Biochem et Biophys Acta , vol.1286 , pp. 1-51
    • Møller, J.C.1    Juul, B.2    Le Maire, M.3
  • 12
    • 0028242939 scopus 로고
    • Wilson disease and Menkes disease: New handles on heavy-metal transport
    • Bull PC, Cox DW. Wilson disease and Menkes disease: new handles on heavy-metal transport. Trends Genet 1994; 10: 246-251.
    • (1994) Trends Genet , vol.10 , pp. 246-251
    • Bull, P.C.1    Cox, D.W.2
  • 13
    • 0027376523 scopus 로고
    • Human Menkes X-chromosome disease and the staphylococcal cadmium-resistance ATPase: A remarkable similarity in protein sequences
    • Silver S, Nucifora G, Phung LT. Human Menkes X-chromosome disease and the staphylococcal cadmium-resistance ATPase: a remarkable similarity in protein sequences. Mol Microbiol 1993; 10: 7-12.
    • (1993) Mol Microbiol , vol.10 , pp. 7-12
    • Silver, S.1    Nucifora, G.2    Phung, L.T.3
  • 14
    • 0028116666 scopus 로고
    • A method to isolate RNA from gram-positive bacteria and mycobacteria
    • Cheung AL, Eberhardt KJ, Fischetti VA. A method to isolate RNA from gram-positive bacteria and mycobacteria. Anal Biochem 1994; 222: 511-514.
    • (1994) Anal Biochem , vol.222 , pp. 511-514
    • Cheung, A.L.1    Eberhardt, K.J.2    Fischetti, V.A.3
  • 17
    • 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 DE. 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 1995; 12: 95-106.
    • (1995) Mol Microbiol , vol.12 , pp. 95-106
    • Ge, Z.1    Hiratsuka, K.2    Taylor, D.E.3
  • 18
    • 0022439117 scopus 로고
    • Organization, expression, and evolution of genes for mercury resistance
    • Summers AO. Organization, expression, and evolution of genes for mercury resistance. Ann Rev Microbiol 1986; 40: 607-634.
    • (1986) Ann Rev Microbiol , vol.40 , pp. 607-634
    • Summers, A.O.1
  • 19
    • 0027288228 scopus 로고
    • Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae
    • Odermatt A, Suter H, Krapf R, Solioz M. Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J Biol Chem 1993; 268: 12775-12779.
    • (1993) J Biol Chem , vol.268 , pp. 12775-12779
    • Odermatt, A.1    Suter, H.2    Krapf, R.3    Solioz, M.4
  • 20
    • 0026094746 scopus 로고
    • Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins
    • Cha J-S, Cooksey DA. Copper resistance in Pseudomonas syringae mediated by periplasmic and outer membrane proteins. Proc Nat Acad Sci USA 1991; 88: 8915-8919.
    • (1991) Proc Nat Acad Sci USA , vol.88 , pp. 8915-8919
    • Cha, J.-S.1    Cooksey, D.A.2
  • 21
    • 0028592629 scopus 로고
    • Novel bacterial P-type ATPases with histidine-rich heavy-metal-associated sequences
    • Trenor C III, Lin W, Andrews NC. Novel bacterial P-type ATPases with histidine-rich heavy-metal-associated sequences. Biochem Biophys Res Comm 1994; 205: 1644-1650.
    • (1994) Biochem Biophys Res Comm , vol.205 , pp. 1644-1650
    • Trenor C. III1    Lin, W.2    Andrews, N.C.3
  • 22
    • 0024348951 scopus 로고
    • Cadmium resistance from Staphylococcus aureus plasmid pI258 cada gene results from a cadium-efflux ATPase
    • Nucifora G, Chu L, Misra TK, Silver S. Cadmium resistance from Staphylococcus aureus plasmid pI258 cadA gene results from a cadium-efflux ATPase. J Bact 1989; 171: 4241-4247.
    • (1989) J Bact , vol.171 , pp. 4241-4247
    • Nucifora, G.1    Chu, L.2    Misra, T.K.3    Silver, S.4
  • 23
    • 0027957289 scopus 로고
    • The immunodominant 38-kDa lipoprotein antigen of Mycobacterium tuberculosis is a phosphate-binding protein
    • Chang ZA, Choudhary R, Lathigra R, Quiocho FA. The immunodominant 38-kDa lipoprotein antigen of Mycobacterium tuberculosis is a phosphate-binding protein. J Biol Chem 1994; 269: 1956-1958.
    • (1994) J Biol Chem , vol.269 , pp. 1956-1958
    • Chang, Z.A.1    Choudhary, R.2    Lathigra, R.3    Quiocho, F.A.4
  • 24
    • 0027468111 scopus 로고
    • Iron-hydroxamate uptake systems in Bacillus subtilis: Identification of a lipoprotein as part of a binding protein-dependent transport system
    • Schneider R, Hantke K. Iron-hydroxamate uptake systems in Bacillus subtilis: identification of a lipoprotein as part of a binding protein-dependent transport system. Mol Microbiol 1993; 8: 111-121.
    • (1993) Mol Microbiol , vol.8 , pp. 111-121
    • Schneider, R.1    Hantke, K.2
  • 25
    • 0027230853 scopus 로고
    • Role of iron in regulation of virulence genes
    • Litwin CM, Calderwood SB. Role of iron in regulation of virulence genes. Clin Microbiol Rev 1993; 6: 137-149.
    • (1993) Clin Microbiol Rev , vol.6 , pp. 137-149
    • Litwin, C.M.1    Calderwood, S.B.2
  • 26
    • 0028825808 scopus 로고
    • Characterization of the Mycobacterium tuberculosis erp gene encoding a potential cell surface protein with repetitive structures
    • Berthet FX, Rauzier J, Lim EM, Philipp W, Gicquel B, Portnoi D. Characterization of the Mycobacterium tuberculosis erp gene encoding a potential cell surface protein with repetitive structures. Microbiol 1995; 141: 2123-2130.
    • (1995) Microbiol , vol.141 , pp. 2123-2130
    • Berthet, F.X.1    Rauzier, J.2    Lim, E.M.3    Philipp, W.4    Gicquel, B.5    Portnoi, D.6
  • 27
    • 0003115434 scopus 로고
    • Mycobacterial gene expression and regulation
    • McFadden J, Ed. London, Surrey University Press
    • Dale JW, Patki A. Mycobacterial gene expression and regulation. In: McFadden J, Ed. Molecular Biology of the Mycobacteria. London, Surrey University Press, 1990: 173-198.
    • (1990) Molecular Biology of the Mycobacteria , pp. 173-198
    • Dale, J.W.1    Patki, A.2
  • 28
    • 0028298234 scopus 로고
    • Purification, characterization, gene sequence, and significance of a bacterioferritin from Mycobacterium leprae
    • Pessolani MVC, Smith DR, Rivoire B, McCormick J, Hefta SA, Cole ST, Brennan PJ. Purification, characterization, gene sequence, and significance of a bacterioferritin from Mycobacterium leprae. J Exp Med 1994; 180: 319-327.
    • (1994) J Exp Med , vol.180 , pp. 319-327
    • Pessolani, M.V.C.1    Smith, D.R.2    Rivoire, B.3    McCormick, J.4    Hefta, S.A.5    Cole, S.T.6    Brennan, P.J.7
  • 29
    • 0028822995 scopus 로고
    • Characterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae
    • Schmitt MP, Predich M, Doukhan L, Smith I, Holmes RK. Characterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae. Infect Immun 1995;63:4284-4289.
    • (1995) Infect Immun , vol.63 , pp. 4284-4289
    • Schmitt, M.P.1    Predich, M.2    Doukhan, L.3    Smith, I.4    Holmes, R.K.5
  • 33
    • 0027446365 scopus 로고
    • Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase
    • Vulpe C, Levinson B, Whitney S, Packman S, Gitschier J. Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nat Genet 1993; 3: 7-13.
    • (1993) Nat Genet , vol.3 , pp. 7-13
    • Vulpe, C.1    Levinson, B.2    Whitney, S.3    Packman, S.4    Gitschier, J.5
  • 34
    • 0040695237 scopus 로고
    • In vitro test with 4,4′-dilsoamyloxythiocarbanilide
    • Eidus L, Hamilton EJ. In vitro test with 4,4′-dilsoamyloxythiocarbanilide. Am Rev Resp Dis 1963;30:258-260.
    • (1963) Am Rev Resp Dis , vol.30 , pp. 258-260
    • Eidus, L.1    Hamilton, E.J.2
  • 35
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • Fish WW. Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Met Enzyme 1988; 158: 357-364.
    • (1988) Met Enzyme , vol.158 , pp. 357-364
    • Fish, W.W.1
  • 36
    • 0014315505 scopus 로고
    • 7H11 medium for the cultivation of mycobacteria
    • Cohn ML. 7H11 medium for the cultivation of mycobacteria. Am Rev Respir Dis 1968; 98: 295-296.
    • (1968) Am Rev Respir Dis , vol.98 , pp. 295-296
    • Cohn, M.L.1
  • 37
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G. Tricine-sodium dodecyl sulfate polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 1983; 166: 368-379.
    • (1983) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 38
    • 0030056239 scopus 로고    scopus 로고
    • Novel insights into the genetics, biochemistry, and immuno-cytochemistry of the 30-kilodalton major extracellular protein of Mycobacterium tuberculosis
    • Harth G, Lee B-Y, Wang J, Clemens DL, Horwitz MA. Novel insights into the genetics, biochemistry, and immuno-cytochemistry of the 30-kilodalton major extracellular protein of Mycobacterium tuberculosis. Infect Immun 1996; 64: 3038-3047.
    • (1996) Infect Immun , vol.64 , pp. 3038-3047
    • Harth, G.1    Lee, B.-Y.2    Wang, J.3    Clemens, D.L.4    Horwitz, M.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.