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Volume 160, Issue 6

Functional diversity of five homologous Cu-ATPases present in Free

Abstract

Copper is an important element in host–microbe interactions, acting both as a catalyst in enzymes and as a potential toxin. Cu-ATPases drive cytoplasmic Cu efflux and protect bacteria against metal overload. Many pathogenic and symbiotic bacteria contain multiple Cu-ATPase genes within particular genetic environments, suggesting alternative roles for each resulting protein. This hypothesis was tested by characterizing five homologous Cu-ATPases present in the symbiotic organism . Mutation of each gene led to different phenotypes and abnormal nodule development in the alfalfa host. Distinct responses were detected in free-living mutant strains exposed to metal and redox stresses. Differential gene expression was detected under Cu, oxygen or nitrosative stress. These observations suggest that CopA1a maintains the cytoplasmic Cu quota and its expression is controlled by Cu levels. CopA1b is also regulated by Cu concentrations and is required during symbiosis for bacteroid maturation. CopA2-like proteins, FixI1 and FixI2, are necessary for the assembly of two different cytochrome oxidases at different stages of bacterial life. CopA3 is a phylogenetically distinct Cu-ATPase that does not contribute to Cu tolerance. It is regulated by redox stress and required during symbiosis. We postulated a model where non-redundant homologous Cu-ATPases, operating under distinct regulation, transport Cu to different target proteins.

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Funding
This study was supported by the:
  • USDA-NIFA Agriculture and Food Research Initiative (Award 2010-65108-20606)
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2014-06-01
2025-05-15
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/content/journal/micro/10.1099/mic.0.079137-0
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Functional diversity of five homologous Cu+-ATPases present in Sinorhizobium meliloti
Microbiology 160, 1237 (2014); https://doi.org/10.1099/mic.0.079137-0
/content/journal/micro/10.1099/mic.0.079137-0
/content/journal/micro/10.1099/mic.0.079137-0
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