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The ATPases CopA and CopB both contribute to copper resistance of the thermoacidophilic archaeon Sulfolobus solfataricus
- Source :
- Microbiology. 158:1622-1633
- Publication Year :
- 2012
- Publisher :
- Microbiology Society, 2012.
-
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.
- Subjects :
- Copper protein
Archaeal Proteins
ATPase
Molecular Sequence Data
ved/biology.organism_classification_rank.species
chemistry.chemical_element
Thermoacidophile
Microbiology
Gene Expression Regulation, Enzymologic
Cofactor
Cytochrome c oxidase
Cation Transport Proteins
Phylogeny
Adenosine Triphosphatases
biology
ved/biology
Sulfolobus solfataricus
Copper
Biochemistry
chemistry
Copper-Transporting ATPases
Copper-transporting ATPases
biology.protein
Reactive Oxygen Species
Subjects
Details
- ISSN :
- 14652080 and 13500872
- Volume :
- 158
- Database :
- OpenAIRE
- Journal :
- Microbiology
- Accession number :
- edsair.doi.dedup.....bc033e81de2c574f30c1cbd4b483ffa0
- Full Text :
- https://doi.org/10.1099/mic.0.055905-0