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Regulation of a novel Acidithiobacillus caldus gene cluster involved in metabolism of reduced inorganic sulfur compounds.
Umeå University.
Center for Bioinformatics and Genome Biology, Life Science Foundation, MIFAB and Andrés Bello University, Santiago, Chile.
Institute of Biochemistry, Vilnius, Lithuania.
Umeå University.
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2007 (English)In: Applied and Environmental Microbiology, ISSN 0099-2240, E-ISSN 1098-5336, Vol. 73, no 22, 7367-7372 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2007. Vol. 73, no 22, 7367-7372 p.
National Category
Microbiology
Research subject
Natural Science, Microbiology
Identifiers
URN: urn:nbn:se:lnu:diva-37333DOI: 10.1128/AEM.01497-07ISI: 000251103300031PubMedID: 17873067OAI: oai:DiVA.org:lnu-37333DiVA: diva2:750370
Available from: 2014-09-29 Created: 2014-09-29 Last updated: 2016-11-30Bibliographically approved

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CiteExportLink to record
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Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • vancouver
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More styles
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  • de-DE
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