Disease relevance of sodA

• Escherichia coli double mutants (sodA sodB) completely lacking superoxide dismutase (SOD) have greatly enhanced mutation rates during aerobic growth [1].
• A SOD mimic protected the sodA sodB strain against the toxicity of erythrose as did the carbonyl-blocking reagents hydrazine and aminoguanidine [2].
• The gene sodA, encoding manganese-containing SOD ([Mn]-SOD), has been cloned from a virulent strain of Haemophilus influenzae type b using degenerate oligonucleotides encoding regions of the gene conserved across different bacterial species [3].
• The S. typhimurium sodA mutant was not significantly attenuated in mice, however, which suggests that resistance to early oxygen-dependent microbicidal mechanisms in vivo may play only a minor role in Salmonella pathogenesis [4].
• One detectable cytoplasmic SOD was identified in the human mucosal pathogen Moraxella catarrhalis, and the gene responsible for the SOD activity, sodA, was isolated from a recent pediatric clinical isolate (strain 7169) [5].

Psychiatry related information on sodA

• The concentrations of immunoreactive Mn SOD and Cu/Zn SOD in the cerebral cortex were not different among the patients with Alzheimer's disease, and the age matched and young patients without neurological disorders [6].

High impact information on sodA

• Strains harboring simultaneous mutations in arcA/B and fur expressed sodA-lacZ under anaerobic growth conditions but were still inducible by iron chelators [7].
• Potential Fnr-binding sites were identified in the promoter region of sodA [7].
• Furthermore, the regulation of sodA by Fur (ferric uptake regulation protein), Arc (aerobic respiratory control), and Fnr (fumarate nitrate reduction/regulator of anaerobic respiration) is independent of the superoxide response regulon SoxRS [7].
• Anacystis nidulans, a cyanobacterium that has no detectable Mn superoxide dismutase and is, consequently, very sensitive to oxidative stress, was also transformed with pMYG1 [8].
• The Mn superoxide dismutase gene of Escherichia coli was subcloned into the E. coli-Anacystis nidulans shuttle vector pSG111 to make the plasmid pMYG1 [8].

Chemical compound and disease context of sodA

• NADPH inhibits transcription of the Escherichia coli manganese superoxide dismutase gene (sodA) in vitro [9].
• The expression of manganese-containing superoxide dismutase (sodA) in Escherichia coli using sodA::lacZ gene fusion was found to be stimulated by DNA gyrase inhibitors, nalidixic acid, or coumermycin A1 [10].
• The recombinant SOD was expressed at high levels in E. coli and protected a sodA sodB double mutant from the toxic effects of methyl viologen [11].
• Transcription of the manganese-superoxide dismutase gene (sodA) in Escherichia coli was shown to be activated by manganese [12].
• Paraquat is known to promote formation of the superoxide radical anion, O2-., and thus the data have been interpreted as indicating that the cloned Mn superoxide dismutase provides protection in both E. coli and A. nidulans against damage attributable to O2-. [8].

Biological context of sodA

• However, the enhanced mutagenesis in aerobically grown sodA sodB mutants is largely dependent on functional exonuclease III, suggesting that the increased flux of superoxide radicals results in DNA lesions that can be acted on by this enzyme, leading to mutations [1].
• Fusion of a 120-base pair fragment, containing 90 base pairs of DNA upstream of the sodA transcription initiation site, to a promoterless galactokinase gene (galK) conferred redox-sensitivity to GalK synthesis [9].
• Erythrose inhibited the growth of a sodA sodB strain of Escherichia coli under aerobiosis; but did not inhibit anaerobic growth of the sodA sodB strain, or the aerobic growth of the superoxide dismutase (SOD)-competent parental strain [2].
• Growth of bacteria under iron-limiting conditions, inactivation of the Fur repressor, or expression of sodA from a plasmid resulted in increased resistance to early killing by J774 cells, which was abolished in the sodA mutant [4].
• The important role of sodA for the pathogenicity of Y. enterocolitica could also be due to detoxification of endogenous, metabolically produced oxygen radicals which are encountered by extracellular enteric pathogens during the invasion of the host [13].

Anatomical context of sodA

• In contrast, inactivation of sodA had only minor effects on survival and multiplication in the gut and Peyer's patches, as could be demonstrated in the orogastric infection model [13].
• A S. typhimurium sodA mutant was created by allelic exchange and tested for the ability to survive in the murine macrophage-like cell line J774 [4].
• Therefore, it appeared likely that the induction of the sodA gene was a response to an increase in superoxide radical production mediated by these membrane-binding drugs in E. coli cells, possibly by disruption of the electron transport systems in the cell membranes [14].
• After allowing for this serum sensitivity difference, the delta sodA delta sodB strain also showed increased susceptibility to phagocytic killing by human neutrophils [15].
• Role of Salmonella typhimurium Mn-superoxide dismutase (SodA) in protection against early killing by J774 macrophages [4].

Associations of sodA with chemical compounds

• A redox buffer containing various ratios of oxidized and reduced glutathione also modulated transcription of sodA thus demonstrating the existence of a redox-sensitive mechanism controlling sodA transcription [9].
• We now report that NADPH, but not NADH, selectively decreases transcription of sodA in vitro and that an NADPH generating system utilizing glucose 6-phosphate and the corresponding dehydrogenase markedly augments this suppressive effect [9].
• Since SOD activity could not be detected in dilute extracts, of the RBO-overexpressing sodA sodB strain, we propose that RBO catalyzes the reduction of O-2 at the expense of cellular reductants such as NAD(P)H [16].
• Maxicell analysis and two-dimensional O'Farrell polyacrylamide gel electrophoresis demonstrated that the structural gene, sodA, of manganese superoxide dismutase was cloned [17].
• The sodA gene was inactivated by insertion of an integrative vector carrying a kanamycin resistance gene [18].

Regulatory relationships of sodA

• A shift to the temperature at which recA441 has constitutive protease activity did not induce Mn-superoxide dismutase but did induce beta-galactosidase [19].

Other interactions of sodA

• Northern blot analysis revealed a transcript that included fumC, orfX, and sodA, the amount of which was increased in response to iron deprivation [20].
• Results on weak oxidative stress promoters (for sodA and acnA genes) were striking in that significant induction was observed when they were under a superoxide stress in plates [21].
• In a comparison with an existing oxidative stress responsive strain, DPD2511 (katG::luxCDABE), which is sensitive to H(2)O(2), the mechanism of chemicals that cause oxidative damage was elucidated via the key transcriptional factors involved in induction of the sodA and katG promoters, i.e. SoxRS and OxyR, respectively [22].

Analytical, diagnostic and therapeutic context of sodA

• The gene encoding Sod, designated sodA, was cloned by the combination of several PCR methods and the Southern hybridization method [23].
• Southern blot analysis also revealed the presence of sodA homologous sequences in Bordetella bronchiseptica [24].
• We used the electrophoretic mobility-shift assay to reveal specific DNA-protein interactions between DNA fragments containing the sodA promoter and proteins present in Escherichia coli cell-free extracts [25].
• The Mn superoxide dismutase polypeptide was identified by electrophoresis on polyacrylamide gels, immunoprecipitation, and the competitive immunoprecipitation effect of pure, active E. coli Mn superoxide dismutase [26].
• Sensitive enzyme immunoassay for human Mn superoxide dismutase [6].

References