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Disease relevance of Thiobacillus


High impact information on Thiobacillus

  • The three-dimensional structure of quinoprotein methylamine dehydrogenase from Thiobacillus versutus has been determined at 2.25 A resolution by a combination of multiple isomorphous replacement, phase extension by solvent flattening and partial structure phasing using molecular dynamics refinement [6].
  • Molecular aspects of the electron transfer system which participates in the oxidation of ferrous ion by Thiobacillus ferrooxidans [7].
  • Here we show that the enzyme from Thiobacillus novellus is a periplasmically located alphabeta heterodimer, consisting of a 40.6-kDa subunit containing a molybdenum cofactor and an 8.8-kDa mono-heme cytochrome c(552) subunit (midpoint redox potential, E(m8.0) = +280 mV) [8].
  • "ADP sulfurylase" from Thiobacillus denitrificans is an adenylylsulfate:phosphate adenylyltransferase and belongs to a new family of nucleotidyltransferases [9].
  • A thiocyanate hydrolase of Thiobacillus thioparus. A novel enzyme catalyzing the formation of carbonyl sulfide from thiocyanate [10].

Chemical compound and disease context of Thiobacillus


Biological context of Thiobacillus

  • The complete amino acid sequence of the blue copper protein amicyanin of Thiobacillus versutus, induced when the bacterium is grown on methylamine, has been determined as follows: QDKITVTSEKPVAAADVPADAVVVGIEKMKYLTPEVTIKAGETVYWVNGEVMPHNVA FKKGIVGEDAFRGEMMTKDQAYAITFNEAGSYDYFCTPHPFMRGKVIVE [15].
  • Isolation and nucleotide sequence of the Thiobacillus ferrooxidans genes for the small and large subunits of ribulose 1,5-bisphosphate carboxylase/oxygenase [16].
  • It has been previously established that Thiobacillus neapolitanus fixes CO2 by using a form I ribulose bisphosphate carboxylase/oxygenase (RuBisCO), that much of the enzyme is sequestered into carboxysomes, and that the genes for the enzyme, cbbL and cbbS, are part of a putative carboxysome operon [17].
  • A recombinant plasmid which contains the gltD gene coding for the glutamate synthase (GOGAT) small subunit was isolated from a Thiobacillus ferrooxidans ATCC33020 gene bank by complementation of an Escherichia coli gltD mutant [18].
  • Based on their structures and the sequences of the inverted terminal repeats and the putative transposase protein, the insertion elements (IS elements) are similar to IST2 of Thiobacillus ferrooxidans and several related elements [19].

Anatomical context of Thiobacillus


Gene context of Thiobacillus

  • A 2089-bp chromosomal DNA segment containing the Thiobacillus ferrooxidans glnA gene has been sequenced [23].
  • The mer operon from a strain of Thiobacillus ferrooxidans (C. Inoue, K. Sugawara, and T. Kusano, Mol. Microbiol. 5:2707-2718, 1991) consists of the regulatory gene merR and an operator-promoter region followed by merC and merA structural genes and differs from other known gram-negative mer operons [24].
  • The alaS gene of Thiobacillus ferrooxidans has been cloned and sequenced and its expression in Escherichia coli and T. ferrooxidans analysed [25].
  • The Thiobacillus ferrooxidans thioredoxin gene, trxA, was isolated by its ability to complement an Escherichia coli gshA trxA mutant which was otherwise unable to grow on minimal medium lacking glutathione [26].
  • The ntrA gene of Thiobacillus ferrooxidans was cloned by complementation of an Escherichia coli ntrA mutant that was unable to produce gas via the sigma 54 (NtrA)-dependent formate hydrogenlyase pathway [1].

Analytical, diagnostic and therapeutic context of Thiobacillus


  1. Complementation of Escherichia coli sigma 54 (NtrA)-dependent formate hydrogenlyase activity by a cloned Thiobacillus ferrooxidans ntrA gene. Berger, D.K., Woods, D.R., Rawlings, D.E. J. Bacteriol. (1990) [Pubmed]
  2. Molecular analysis of the Bacteroides fragilis recA gene. Goodman, H.J., Woods, D.R. Gene (1990) [Pubmed]
  3. Anaerobic versus aerobic degradation of dimethyl sulfide and methanethiol in anoxic freshwater sediments. Lomans, B.P., den Camp, H.J., Pol, A., Vogels, G.D. Appl. Environ. Microbiol. (1999) [Pubmed]
  4. Ethanolamine utilization in Salmonella typhimurium: nucleotide sequence, protein expression, and mutational analysis of the cchA cchB eutE eutJ eutG eutH gene cluster. Stojiljkovic, I., Bäumler, A.J., Heffron, F. J. Bacteriol. (1995) [Pubmed]
  5. Characterization of IS1201, an insertion sequence isolated from Lactobacillus helveticus. Tailliez, P., Ehrlich, S.D., Chopin, M.C. Gene (1994) [Pubmed]
  6. Structure of quinoprotein methylamine dehydrogenase at 2.25 A resolution. Vellieux, F.M., Huitema, F., Groendijk, H., Kalk, K.H., Jzn, J.F., Jongejan, J.A., Duine, J.A., Petratos, K., Drenth, J., Hol, W.G. EMBO J. (1989) [Pubmed]
  7. Molecular aspects of the electron transfer system which participates in the oxidation of ferrous ion by Thiobacillus ferrooxidans. Yamanaka, T., Fukumori, Y. FEMS Microbiol. Rev. (1995) [Pubmed]
  8. Sulfite:Cytochrome c oxidoreductase from Thiobacillus novellus. Purification, characterization, and molecular biology of a heterodimeric member of the sulfite oxidase family. Kappler, U., Bennett, B., Rethmeier, J., Schwarz, G., Deutzmann, R., McEwan, A.G., Dahl, C. J. Biol. Chem. (2000) [Pubmed]
  9. "ADP sulfurylase" from Thiobacillus denitrificans is an adenylylsulfate:phosphate adenylyltransferase and belongs to a new family of nucleotidyltransferases. Brüser, T., Selmer, T., Dahl, C. J. Biol. Chem. (2000) [Pubmed]
  10. A thiocyanate hydrolase of Thiobacillus thioparus. A novel enzyme catalyzing the formation of carbonyl sulfide from thiocyanate. Katayama, Y., Narahara, Y., Inoue, Y., Amano, F., Kanagawa, T., Kuraishi, H. J. Biol. Chem. (1992) [Pubmed]
  11. Respiratory enzymes of Thiobacillus ferrooxidans. A kinetic study of electron transfer between iron and rusticyanin in sulfate media. Blake, R.C., Shute, E.A. J. Biol. Chem. (1987) [Pubmed]
  12. Mössbauer and EPR studies on nitrite reductase from Thiobacillus denitrificans. Huynh, B.H., Lui, M.C., Moura, J.J., Moura, I., Ljungdahl, P.O., Münck, E., Payne, W.J., Peck, H.D., DerVartanian, D.V., LeGall, J. J. Biol. Chem. (1982) [Pubmed]
  13. Mutagenesis of the conserved lysine 14 of cytochrome c-550 from Thiobacillus versutus affects the protein structure and the electron self-exchange rate. Ubbink, M., Canters, G.W. Biochemistry (1993) [Pubmed]
  14. Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus. Gorren, A.C., Moenne-Loccoz, P., Backes, G., de Vries, S., Sanders-Loehr, J., Duine, J.A. Biochemistry (1995) [Pubmed]
  15. The structural homology of amicyanin from Thiobacillus versutus to plant plastocyanins. Van Beeumen, J., Van Bun, S., Canters, G.W., Lommen, A., Chothia, C. J. Biol. Chem. (1991) [Pubmed]
  16. Isolation and nucleotide sequence of the Thiobacillus ferrooxidans genes for the small and large subunits of ribulose 1,5-bisphosphate carboxylase/oxygenase. Pulgar, V., Gaete, L., Allende, J., Orellana, O., Jordana, X., Jedlicki, E. FEBS Lett. (1991) [Pubmed]
  17. Insertion mutation of the form I cbbL gene encoding ribulose bisphosphate carboxylase/oxygenase (RuBisCO) in Thiobacillus neapolitanus results in expression of form II RuBisCO, loss of carboxysomes, and an increased CO2 requirement for growth. Baker, S.H., Jin, S., Aldrich, H.C., Howard, G.T., Shively, J.M. J. Bacteriol. (1998) [Pubmed]
  18. Cloning and sequencing of the gene for the Thiobacillus ferrooxidans ATCC33020 glutamate synthase (GOGAT) small subunit and complementation of an Escherichia coli gltD mutant. Deane, S.M., Rawlings, D.E. Gene (1996) [Pubmed]
  19. A fusion promoter created by a new insertion sequence, IS1490, activates transcription of 2,4,5-trichlorophenoxyacetic acid catabolic genes in Burkholderia cepacia AC1100. Hübner, A., Hendrickson, W. J. Bacteriol. (1997) [Pubmed]
  20. Effect of divers anions on the electron-transfer reaction between iron and rusticyanin from Thiobacillus ferrooxidans. Blake, R.C., White, K.J., Shute, E.A. Biochemistry (1991) [Pubmed]
  21. D-Ribulose-1,5-bisphosphate carboxylase and polyhedral inclusion bodies in Thiobacillus intermedius. Purohit, K., McFadden, B.A., Shaykh, M.M. J. Bacteriol. (1976) [Pubmed]
  22. Ferrous iron-dependent volatilization of mercury by the plasma membrane of Thiobacillus ferrooxidans. Iwahori, K., Takeuchi, F., Kamimura, K., Sugio, T. Appl. Environ. Microbiol. (2000) [Pubmed]
  23. Nucleotide sequence of the glutamine synthetase gene and its controlling region from the acidophilic autotroph Thiobacillus ferrooxidans. Rawlings, D.E., Jones, W.A., O'Neill, E.G., Woods, D.R. Gene (1987) [Pubmed]
  24. Electrotransformation of Thiobacillus ferrooxidans with plasmids containing a mer determinant. Kusano, T., Sugawara, K., Inoue, C., Takeshima, T., Numata, M., Shiratori, T. J. Bacteriol. (1992) [Pubmed]
  25. Alanyl-tRNA synthetase gene of the extreme acidophilic chemolithoautotrophic Thiobacillus ferrooxidans is highly homologous to alaS genes from all living kingdoms but cannot be transcribed from its promoter in Escherichia coli. Guiliani, N., Bengrine, A., Borne, F., Chippaux, M., Bonnefoy, V. Microbiology (Reading, Engl.) (1997) [Pubmed]
  26. Molecular genetic analysis of a thioredoxin gene from Thiobacillus ferrooxidans. Powles, R.E., Deane, S.M., Rawlings, D.E. Microbiology (Reading, Engl.) (1995) [Pubmed]
  27. Molecular cloning of the gene encoding Thiobacillus ferrooxidans Fe(II) oxidase. High homology of the gene product with HiPIP. Kusano, T., Takeshima, T., Sugawara, K., Inoue, C., Shiratori, T., Yano, T., Fukumori, Y., Yamanaka, T. J. Biol. Chem. (1992) [Pubmed]
  28. Bacterial oxidation of polythionates: determination of tetrathionate with an ion-selective electrode. Tuovinen, O.H., Nicholas, D.J. Appl. Environ. Microbiol. (1977) [Pubmed]
  29. Effect of particle-particle shearing on the bioleaching of sulfide minerals. Chong, N., Karamanev, D.G., Margaritis, A. Biotechnol. Bioeng. (2002) [Pubmed]
  30. Equilibrium of the reaction between dissolved sodium sulfide and biologically produced sulfur. Kleinjan, W.E., de Keizer, A., Janssen, A.J. Colloids and surfaces. B, Biointerfaces. (2005) [Pubmed]
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