Sulfur metabolism in the extreme acidophile Acidithiobacillus caldus

Stefanie Mangold, Jorge Valdés, David S. Holmes, Mark Dopson

Resultado de la investigación: Article

85 Citas (Scopus)

Resumen

Given the challenges to life at low pH, an analysis of inorganic sulfur compound (ISC) oxidation was initiated in the chemolithoautotrophic extremophile Acidithiobacillus caldus. A. caldus is able to metabolize elemental sulfur and a broad range of ISCs. It has been implicated in the production of environmentally damaging acidic solutions as well as participating in industrial bioleaching operations where it forms part of microbial consortia used for the recovery of metal ions. Based upon the recently published A. caldus type strain genome sequence, a bioinformatic reconstruction of elemental sulfur and ISC metabolism predicted genes included: sulfide-quinone reductase (sqr), tetrathionate hydrolase (tth), two sox gene clusters potentially involved in thiosulfate oxidation (soxABXYZ), sulfur oxygenase reductase (sor), and various electron transport components. RNA transcript profiles by semi quantitative reverse transcription PCR suggested up-regulation of sox genes in the presence of tetrathionate. Extensive gel based proteomic comparisons of total soluble and membrane enriched protein fractions during growth on elemental sulfur and tetrathionate identified differential protein levels from the two Sox clusters as well as several chaperone and stress proteins up-regulated in the presence of elemental sulfur. Proteomics results also suggested the involvement of heterodisulfide reductase (HdrABC) in A. caldus ISC metabolism. A putative new function of Hdr in acidophiles is discussed. Additional proteomic analysis evaluated protein expression differences between cells grown attached to solid, elemental sulfur versus planktonic cells. This study has provided insights into sulfur metabolism of this acidophilic chemolithotroph and gene expression during attachment to solid elemental sulfur.

Idioma originalEnglish
PublicaciónFrontiers in Microbiology
Volumen2
N.ºFEB
DOI
EstadoPublished - 2011

Huella dactilar

Acidithiobacillus
Sulfur
Sulfur Compounds
Proteomics
sulfide quinone reductase
Microbial Consortia
Thiosulfates
Oxygenases
Multigene Family
Electron Transport
Heat-Shock Proteins
Computational Biology
Genes
Reverse Transcription
Membrane Proteins
Proteins
Up-Regulation
Gels
Metals
Genome

ASJC Scopus subject areas

  • Microbiology
  • Microbiology (medical)

Citar esto

Mangold, Stefanie ; Valdés, Jorge ; Holmes, David S. ; Dopson, Mark. / Sulfur metabolism in the extreme acidophile Acidithiobacillus caldus. En: Frontiers in Microbiology. 2011 ; Vol. 2, N.º FEB.
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Sulfur metabolism in the extreme acidophile Acidithiobacillus caldus. / Mangold, Stefanie; Valdés, Jorge; Holmes, David S.; Dopson, Mark.

En: Frontiers in Microbiology, Vol. 2, N.º FEB, 2011.

Resultado de la investigación: Article

TY - JOUR

T1 - Sulfur metabolism in the extreme acidophile Acidithiobacillus caldus

AU - Mangold, Stefanie

AU - Valdés, Jorge

AU - Holmes, David S.

AU - Dopson, Mark

PY - 2011

Y1 - 2011

N2 - Given the challenges to life at low pH, an analysis of inorganic sulfur compound (ISC) oxidation was initiated in the chemolithoautotrophic extremophile Acidithiobacillus caldus. A. caldus is able to metabolize elemental sulfur and a broad range of ISCs. It has been implicated in the production of environmentally damaging acidic solutions as well as participating in industrial bioleaching operations where it forms part of microbial consortia used for the recovery of metal ions. Based upon the recently published A. caldus type strain genome sequence, a bioinformatic reconstruction of elemental sulfur and ISC metabolism predicted genes included: sulfide-quinone reductase (sqr), tetrathionate hydrolase (tth), two sox gene clusters potentially involved in thiosulfate oxidation (soxABXYZ), sulfur oxygenase reductase (sor), and various electron transport components. RNA transcript profiles by semi quantitative reverse transcription PCR suggested up-regulation of sox genes in the presence of tetrathionate. Extensive gel based proteomic comparisons of total soluble and membrane enriched protein fractions during growth on elemental sulfur and tetrathionate identified differential protein levels from the two Sox clusters as well as several chaperone and stress proteins up-regulated in the presence of elemental sulfur. Proteomics results also suggested the involvement of heterodisulfide reductase (HdrABC) in A. caldus ISC metabolism. A putative new function of Hdr in acidophiles is discussed. Additional proteomic analysis evaluated protein expression differences between cells grown attached to solid, elemental sulfur versus planktonic cells. This study has provided insights into sulfur metabolism of this acidophilic chemolithotroph and gene expression during attachment to solid elemental sulfur.

AB - Given the challenges to life at low pH, an analysis of inorganic sulfur compound (ISC) oxidation was initiated in the chemolithoautotrophic extremophile Acidithiobacillus caldus. A. caldus is able to metabolize elemental sulfur and a broad range of ISCs. It has been implicated in the production of environmentally damaging acidic solutions as well as participating in industrial bioleaching operations where it forms part of microbial consortia used for the recovery of metal ions. Based upon the recently published A. caldus type strain genome sequence, a bioinformatic reconstruction of elemental sulfur and ISC metabolism predicted genes included: sulfide-quinone reductase (sqr), tetrathionate hydrolase (tth), two sox gene clusters potentially involved in thiosulfate oxidation (soxABXYZ), sulfur oxygenase reductase (sor), and various electron transport components. RNA transcript profiles by semi quantitative reverse transcription PCR suggested up-regulation of sox genes in the presence of tetrathionate. Extensive gel based proteomic comparisons of total soluble and membrane enriched protein fractions during growth on elemental sulfur and tetrathionate identified differential protein levels from the two Sox clusters as well as several chaperone and stress proteins up-regulated in the presence of elemental sulfur. Proteomics results also suggested the involvement of heterodisulfide reductase (HdrABC) in A. caldus ISC metabolism. A putative new function of Hdr in acidophiles is discussed. Additional proteomic analysis evaluated protein expression differences between cells grown attached to solid, elemental sulfur versus planktonic cells. This study has provided insights into sulfur metabolism of this acidophilic chemolithotroph and gene expression during attachment to solid elemental sulfur.

KW - Acidithiobacillus caldus

KW - Attachment

KW - Elemental sulfur

KW - Inorganic sulfur compounds

KW - Metabolism

KW - Proteomics

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M3 - Article

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JO - Frontiers in Microbiology

JF - Frontiers in Microbiology

SN - 1664-302X

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