ArticleJournal of bacteriology2001
Identification and characterization of a second superoxide dismutase gene (sodM) from Staphylococcus aureus.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 77 citations in OpenAlex.
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- Copper primes adaptation of uropathogenic Escherichia coli to superoxide stress by activating superoxide dismutases.PLoS pathogens · 2020Article
- What Happens in the Staphylococcal Nucleoid under Oxidative Stress?Microorganisms · 2019Review
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- RsaC sRNA modulates the oxidative stress response of Staphylococcus aureus during manganese starvation.Nucleic acids research · 2019Article
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- MntC-Dependent Manganese Transport Is Essential formSphere · 2018Article
- Comparative Proteomic and Morphological Change Analyses ofFrontiers in microbiology · 2018Article
- Identification of nucleoid associated proteins (NAPs) under oxidative stress in Staphylococcus aureus.BMC microbiology · 2017Article
- A Superoxide Dismutase Capable of Functioning with Iron or Manganese Promotes the Resistance of Staphylococcus aureus to Calprotectin and Nutritional Immunity.PLoS pathogens · 2017Article
- Epic Immune Battles of History: Neutrophils vs.Frontiers in cellular and infection microbiology · 2017Review
- Bacillithiol has a role in Fe-S cluster biogenesis in Staphylococcus aureus.Molecular microbiology · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
A gene encoding superoxide dismutase (SOD), sodM, from S. aureus was cloned and characterized. The deduced amino acid sequence specifies a 187-amino-acid protein with 75% identity to the S. aureus SodA protein. Amino acid sequence comparisons with known SODs and relative insensitivity to hydrogen peroxide and potassium cyanide indicate that SodM most likely uses manganese (Mn) as a cofactor. The sodM gene expressed from a plasmid rescued an Escherichia coli double mutant (sodA sodB) under conditions that are otherwise lethal. SOD activity gels of S. aureus RN6390 whole-cell lysates revealed three closely migrating bands of activity. The two upper bands were absent in a sodM mutant, while the two lower bands were absent in a sodA mutant. Thus, the middle band of activity most likely represents a SodM-SodA hybrid protein. All three bands of activity increased as highly aerated cultures entered the late exponential phase of growth, SodM more so than SodA. Viability of the sodA and sodM sodA mutants but not the sodM mutant was drastically reduced under oxidative stress conditions generated by methyl viologen (MV) added during the early exponential phase of growth. However, only the viability of the sodM sodA mutant was reduced when MV was added during the late exponential and stationary phases of growth. These data indicate that while SodA may be the major SOD activity in S. aureus throughout all stages of growth, SodM, under oxidative stress, becomes a major source of activity during the late exponential and stationary phases of growth such that viability and growth of an S. aureus sodA mutant are maintained.
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