The ATPases CopA and CopB both contribute to copper resistance of the thermoacidophilic archaeon Sulfolobus solfataricus

Certain heavy metal ions such as copper and zinc serve as essential cofactors of many enzymes, but are toxic at high concentrations. Thus, intracellular levels have to be subtly balanced. P-type ATPases of the P(IB)-subclass play a major role in metal homeostasis. The thermoacidophile Sulfolobus sol...

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Published inMicrobiology (Society for General Microbiology) Vol. 158; no. Pt 6; pp. 1622 - 1633
Main Authors VÖLLMECKE, Christian, DREES, Steffen L, REIMANN, Julia, ALBERS, Sonja-Verena, LÜBBEN, Mathias
Format Journal Article
LanguageEnglish
Published Reading Society for General Microbiology 01.06.2012
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Abstract Certain heavy metal ions such as copper and zinc serve as essential cofactors of many enzymes, but are toxic at high concentrations. Thus, intracellular levels have to be subtly balanced. P-type ATPases of the P(IB)-subclass play a major role in metal homeostasis. The thermoacidophile Sulfolobus solfataricus possesses two P(IB)-ATPases named CopA and CopB. Both enzymes are present in cells grown in copper-depleted medium and are accumulated upon an increase in the external copper concentration. We studied the physiological roles of both ATPases by disrupting genes copA and copB. Neither of them affected the sensitivity of S. solfataricus to reactive oxygen species, nor were they a strict prerequisite to the biosynthesis of the copper protein cytochrome oxidase. Deletion mutant analysis demonstrated that CopA is an effective copper pump at low and high copper concentrations. CopB appeared to be a low-affinity copper export ATPase, which was only relevant if the media copper concentration was exceedingly high. CopA and CopB thus act as resistance factors to copper ions at overlapping concentrations. Moreover, growth tests on solid media indicated that both ATPases are involved in resistance to silver.
AbstractList Certain heavy metal ions such as copper and zinc serve as essential cofactors of many enzymes, but are toxic at high concentrations. Thus, intracellular levels have to be subtly balanced. P-type ATPases of the P(IB)-subclass play a major role in metal homeostasis. The thermoacidophile Sulfolobus solfataricus possesses two P(IB)-ATPases named CopA and CopB. Both enzymes are present in cells grown in copper-depleted medium and are accumulated upon an increase in the external copper concentration. We studied the physiological roles of both ATPases by disrupting genes copA and copB. Neither of them affected the sensitivity of S. solfataricus to reactive oxygen species, nor were they a strict prerequisite to the biosynthesis of the copper protein cytochrome oxidase. Deletion mutant analysis demonstrated that CopA is an effective copper pump at low and high copper concentrations. CopB appeared to be a low-affinity copper export ATPase, which was only relevant if the media copper concentration was exceedingly high. CopA and CopB thus act as resistance factors to copper ions at overlapping concentrations. Moreover, growth tests on solid media indicated that both ATPases are involved in resistance to silver.
Author ALBERS, Sonja-Verena
LÜBBEN, Mathias
VÖLLMECKE, Christian
REIMANN, Julia
DREES, Steffen L
Author_xml – sequence: 1
  givenname: Christian
  surname: VÖLLMECKE
  fullname: VÖLLMECKE, Christian
  organization: Lehrstuhl für Biophysik, Ruhr-Universität Bochum, Universitätsstr. 150, 44780 Bochum, Germany
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  givenname: Steffen L
  surname: DREES
  fullname: DREES, Steffen L
  organization: Lehrstuhl für Biophysik, Ruhr-Universität Bochum, Universitätsstr. 150, 44780 Bochum, Germany
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  givenname: Julia
  surname: REIMANN
  fullname: REIMANN, Julia
  organization: Molecular Biology of Archaea, MPI für Terrestrische Mikrobiologie, Marburg, Karl-von-Frisch-Strasse 10, 35043 Marburg, Germany
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  givenname: Sonja-Verena
  surname: ALBERS
  fullname: ALBERS, Sonja-Verena
  organization: Molecular Biology of Archaea, MPI für Terrestrische Mikrobiologie, Marburg, Karl-von-Frisch-Strasse 10, 35043 Marburg, Germany
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  givenname: Mathias
  surname: LÜBBEN
  fullname: LÜBBEN, Mathias
  organization: Lehrstuhl für Biophysik, Ruhr-Universität Bochum, Universitätsstr. 150, 44780 Bochum, Germany
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Issue Pt 6
Keywords Acidophily
Enzyme
Archaeobacteria
Adenosinetriphosphatase
Thermophily
Sulfolobus solfataricus
Heavy metal
Resistance
Sulfolobaceae
Bacteria
Hydrolases
Sulfolobales
Copper
Language English
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Snippet Certain heavy metal ions such as copper and zinc serve as essential cofactors of many enzymes, but are toxic at high concentrations. Thus, intracellular levels...
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StartPage 1622
SubjectTerms Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
Archaeal Proteins - genetics
Archaeal Proteins - metabolism
Bacteriology
Biological and medical sciences
Cation Transport Proteins - genetics
Cation Transport Proteins - metabolism
Copper - metabolism
Copper-Transporting ATPases
Fundamental and applied biological sciences. Psychology
Gene Expression Regulation, Enzymologic
Microbiology
Miscellaneous
Molecular Sequence Data
Phylogeny
Reactive Oxygen Species - metabolism
Sulfolobus solfataricus - classification
Sulfolobus solfataricus - enzymology
Sulfolobus solfataricus - genetics
Sulfolobus solfataricus - metabolism
Title The ATPases CopA and CopB both contribute to copper resistance of the thermoacidophilic archaeon Sulfolobus solfataricus
URI https://www.ncbi.nlm.nih.gov/pubmed/22361944
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