Regulation of a novel Acidithiobacillus caldus gene cluster involved in metabolism of reduced inorganic sulfur compounds

Olena I. Rzhepishevska, Jorge Valdés, Liucija Marcinkeviciene, Camelia Algora Gallardo, Rolandas Meskys, Violaine Bonnefoy, David S. Holmes, Mark Dopson

Resultado de la investigación: Article

38 Citas (Scopus)

Resumen

Acidithiobacillus caldus has been proposed to play a role in the oxidation of reduced inorganic sulfur compounds (RISCs) produced in industrial biomining of sulfidic minerals. Here, we describe the regulation of a new cluster containing the gene encoding tetrathionate hydrolase (tetH), a key enzyme in the RISC metabolism of this bacterium. The cluster contains five cotranscribed genes, ISac1, rsrR, rsrS, tetH, and doxD, coding for a transposase, a two-component response regulator (RsrR and RsrS), tetrathionate hydrolase, and DoxD, respectively. As shown by quantitative PCR, rsrR, tetH, and doxD are upregulated to different degrees in the presence of tetrathionate. Western blot analysis also indicates upregulation of TetH in the presence of tetrathionate, thiosulfate, and pyrite. The tetH cluster is predicted to have two promoters, both of which are functional in Escherichia coli and one of which was mapped by primer extension. A pyrrolo-quinoline quinone binding domain in TetH was predicted by bioinformatic analysis, and the presence of an o-quinone moiety was experimentally verified, suggesting a mechanism for tetrathionate oxidation.

Idioma originalEnglish
Páginas (desde-hasta)7367-7372
Número de páginas6
PublicaciónApplied and Environmental Microbiology
Volumen73
N.º22
DOI
EstadoPublished - nov 2007

Huella dactilar

Acidithiobacillus caldus
Acidithiobacillus
Sulfur Compounds
sulfur compound
Multigene Family
hydrolases
multigene family
sulfur
metabolism
oxidation
bioinformatics
gene
thiosulfate
pyrite
quinones
enzyme
PQQ Cofactor
bacterium
Transposases
quinoline

ASJC Scopus subject areas

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

Citar esto

Rzhepishevska, O. I., Valdés, J., Marcinkeviciene, L., Gallardo, C. A., Meskys, R., Bonnefoy, V., ... Dopson, M. (2007). Regulation of a novel Acidithiobacillus caldus gene cluster involved in metabolism of reduced inorganic sulfur compounds. Applied and Environmental Microbiology, 73(22), 7367-7372. https://doi.org/10.1128/AEM.01497-07
Rzhepishevska, Olena I. ; Valdés, Jorge ; Marcinkeviciene, Liucija ; Gallardo, Camelia Algora ; Meskys, Rolandas ; Bonnefoy, Violaine ; Holmes, David S. ; Dopson, Mark. / Regulation of a novel Acidithiobacillus caldus gene cluster involved in metabolism of reduced inorganic sulfur compounds. En: Applied and Environmental Microbiology. 2007 ; Vol. 73, N.º 22. pp. 7367-7372.
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abstract = "Acidithiobacillus caldus has been proposed to play a role in the oxidation of reduced inorganic sulfur compounds (RISCs) produced in industrial biomining of sulfidic minerals. Here, we describe the regulation of a new cluster containing the gene encoding tetrathionate hydrolase (tetH), a key enzyme in the RISC metabolism of this bacterium. The cluster contains five cotranscribed genes, ISac1, rsrR, rsrS, tetH, and doxD, coding for a transposase, a two-component response regulator (RsrR and RsrS), tetrathionate hydrolase, and DoxD, respectively. As shown by quantitative PCR, rsrR, tetH, and doxD are upregulated to different degrees in the presence of tetrathionate. Western blot analysis also indicates upregulation of TetH in the presence of tetrathionate, thiosulfate, and pyrite. The tetH cluster is predicted to have two promoters, both of which are functional in Escherichia coli and one of which was mapped by primer extension. A pyrrolo-quinoline quinone binding domain in TetH was predicted by bioinformatic analysis, and the presence of an o-quinone moiety was experimentally verified, suggesting a mechanism for tetrathionate oxidation.",
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Rzhepishevska, OI, Valdés, J, Marcinkeviciene, L, Gallardo, CA, Meskys, R, Bonnefoy, V, Holmes, DS & Dopson, M 2007, 'Regulation of a novel Acidithiobacillus caldus gene cluster involved in metabolism of reduced inorganic sulfur compounds', Applied and Environmental Microbiology, vol. 73, n.º 22, pp. 7367-7372. https://doi.org/10.1128/AEM.01497-07

Regulation of a novel Acidithiobacillus caldus gene cluster involved in metabolism of reduced inorganic sulfur compounds. / Rzhepishevska, Olena I.; Valdés, Jorge; Marcinkeviciene, Liucija; Gallardo, Camelia Algora; Meskys, Rolandas; Bonnefoy, Violaine; Holmes, David S.; Dopson, Mark.

En: Applied and Environmental Microbiology, Vol. 73, N.º 22, 11.2007, p. 7367-7372.

Resultado de la investigación: Article

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AU - Rzhepishevska, Olena I.

AU - Valdés, Jorge

AU - Marcinkeviciene, Liucija

AU - Gallardo, Camelia Algora

AU - Meskys, Rolandas

AU - Bonnefoy, Violaine

AU - Holmes, David S.

AU - Dopson, Mark

PY - 2007/11

Y1 - 2007/11

N2 - Acidithiobacillus caldus has been proposed to play a role in the oxidation of reduced inorganic sulfur compounds (RISCs) produced in industrial biomining of sulfidic minerals. Here, we describe the regulation of a new cluster containing the gene encoding tetrathionate hydrolase (tetH), a key enzyme in the RISC metabolism of this bacterium. The cluster contains five cotranscribed genes, ISac1, rsrR, rsrS, tetH, and doxD, coding for a transposase, a two-component response regulator (RsrR and RsrS), tetrathionate hydrolase, and DoxD, respectively. As shown by quantitative PCR, rsrR, tetH, and doxD are upregulated to different degrees in the presence of tetrathionate. Western blot analysis also indicates upregulation of TetH in the presence of tetrathionate, thiosulfate, and pyrite. The tetH cluster is predicted to have two promoters, both of which are functional in Escherichia coli and one of which was mapped by primer extension. A pyrrolo-quinoline quinone binding domain in TetH was predicted by bioinformatic analysis, and the presence of an o-quinone moiety was experimentally verified, suggesting a mechanism for tetrathionate oxidation.

AB - Acidithiobacillus caldus has been proposed to play a role in the oxidation of reduced inorganic sulfur compounds (RISCs) produced in industrial biomining of sulfidic minerals. Here, we describe the regulation of a new cluster containing the gene encoding tetrathionate hydrolase (tetH), a key enzyme in the RISC metabolism of this bacterium. The cluster contains five cotranscribed genes, ISac1, rsrR, rsrS, tetH, and doxD, coding for a transposase, a two-component response regulator (RsrR and RsrS), tetrathionate hydrolase, and DoxD, respectively. As shown by quantitative PCR, rsrR, tetH, and doxD are upregulated to different degrees in the presence of tetrathionate. Western blot analysis also indicates upregulation of TetH in the presence of tetrathionate, thiosulfate, and pyrite. The tetH cluster is predicted to have two promoters, both of which are functional in Escherichia coli and one of which was mapped by primer extension. A pyrrolo-quinoline quinone binding domain in TetH was predicted by bioinformatic analysis, and the presence of an o-quinone moiety was experimentally verified, suggesting a mechanism for tetrathionate oxidation.

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