An Iron-containing Superoxide Dismutase from Escherichia coli

Yost, Fred J.; Fridovich, Irwin

doi:10.1016/s0021-9258(19)43649-1

Cited by 355 publications

(36 citation statements)

References 29 publications

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“…Thus, superoxide dismutase, catalase and peroxidases constitute important defense mechanisms against toxic oxygen free radicals (1-7). E. coli cells can synthesize two distinct types of superoxide dismutase, one containing manganese (9), and the other iron (10). Iron-superoxide dismutase (Fe-SOD) is synthesized constitutively under most growth conditions including anaerobiosis, whereas the level of manganese-superoxide dismutase (Mn-SOD) inside the cell varies widely according to the growth conditions (3,(11)(12)(13)(14)(15).…”

Section: Introductionmentioning

confidence: 99%

Structure and gene expression of theE. coliMn-superoxide dismutase gene

1986

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Superoxide dismutase is an enzyme which converts superoxide O2- to hydrogen peroxide. Using a single synthetic oligonucleotide 33mer, we screened the E. coli DNA library and isolated a clone containing the E. coli manganese-superoxide dismutase gene. We determined the DNA sequence. The analysis of the DNA sequence and in vivo as well as in vitro transcription has shown the following. The DNA sequence suggests two possible promoters. However, only one of them seems active during normal aerobic growth. Purified RNA polymerase initiates in vitro transcription from the same promoter. It is not clear whether the second promoter is functional. It is possible that this promoter could be activated under different growth conditions. There is an inverted repeat sequence which could form a stem-loop structure downstream of the translation stop codon TAA of the Mn-SOD gene. The results of the analysis of in vivo and in vitro RNA have shown that this is the transcription termination signal. Thus, the Mn-SOD gene constitutes a single gene operon. There is an almost perfect 19 base palindrome at the -35 region. The position and the size of the palindrome suggest that this could be a regulatory site.

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Section: Introductionmentioning

confidence: 99%

Structure and gene expression of theE. coliMn-superoxide dismutase gene

1986

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“…SodB is a mononuclear iron containing enzyme that has been found to be a relatively abundant protein (around 1% of total protein) in E. coli. 15,16 E. coli contains three different superoxide dismutases: Mn containing SodA, Fe containing SodB and CuZn containing SodC. SodA and SodC are induced under aerobic conditions, SodB is present under both aerobic and anaerobic conditions.…”

Section: Resultsmentioning

confidence: 99%

Exploring the microbial metalloproteome using MIRAGE

et al. 2011

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The microbial metalloproteome has been largely unexplored. Using the metalloproteomics approach MIRAGE (Metal Isotope native RadioAutography in Gel Electrophoresis) we have been able to explore the soluble Fe and Zn metalloproteome of Escherichia coli. The protein identification by MS/MS typically resulted in several overlapping proteins for each metal containing spot. Using the E. coli genome annotation the proteins relevant to the iron and zinc proteome were selected. Superoxide dismutase (SodB) was found to be the major iron protein after cultivation with a normal iron concentration of 6 μM. Upon an elevated iron concentration of 40 μM, ferritin (FtnA) became dominant. Under both conditions 90% of the iron was associated with just three different proteins: superoxide dismutase (SodB), ferritin (FtnA) and bacterioferritin (Bfr). The uncharacterized proteins YgfK and XdhD were found to be significant iron containing proteins under elevated iron conditions. The zinc proteome of E. coli experiencing zinc stress was dominated by ZraP, a putative zinc storage protein.

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“…While the true antiquity of these three enzyme families is not known with certainty, the relative ages have been inferred from a combination of phylogenetic arguments and likely environmental conditions on the ancient surface Earth. The FeSOD/MnSOD enzyme family is thought to be the most ancient of these three enzyme families (Hatchikian & Henry, 1977; Yost & Fridovich, 1973). This notion is evidenced by the observation that sodA/sodB is phylogenetically wide‐spread, and because low atmospheric oxygen in the early Earth would have favored high concentrations of dissolved Fe 2+ and Mn 2+ (Wolfe‐Simon et al., 2005).…”

Section: Introductionmentioning

confidence: 99%

Inter‐domain horizontal gene transfer of nickel‐binding superoxide dismutase

et al. 2021

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The ability of aerobic microorganisms to regulate internal and external concentrations of the reactive oxygen species (ROS) superoxide directly influences the health and viability of cells. Superoxide dismutases (SODs) are the primary regulatory enzymes that are used by microorganisms to degrade superoxide. SOD is not one, but three separate, non‐homologous enzymes that perform the same function. Thus, the evolutionary history of genes encoding for different SOD enzymes is one of convergent evolution, which reflects environmental selection brought about by an oxygenated atmosphere, changes in metal availability, and opportunistic horizontal gene transfer (HGT). In this study, we examine the phylogenetic history of the protein sequence encoding for the nickel‐binding metalloform of the SOD enzyme (SodN). The genomic potential to produce SodN is widespread among bacteria, including Actinobacteriota (Actinobacteria), Chloroflexota (Chloroflexi), Cyanobacteria, Proteobacteria, Patescibacteria, and others. The gene is also present in many archaea, with Thermoplasmatota and Nanoarchaeota representing the vast majority of archaeal sodN diversity. A comparison of organismal and SodN protein phylogenetic trees reveals several instances of HGT, including multiple inter‐domain transfers of the sodN gene from the bacterial domain to the archaeal domain. Nearly half of the archaeal members with sodN live in the photic zone of the marine water column. The sodN gene is widespread and characterized by apparent vertical gene transfer in some sediment‐ or soil‐associated lineages within the Actinobacteriota and Chloroflexota phyla, suggesting the ancestral sodN likely originated in one of these clades before expanding its taxonomic and biogeographic distribution to additional microbial groups in the surface ocean in response to decreasing iron availability. In addition to decreasing iron quotas, nickel‐binding SOD has the added benefit of withstanding high reactant and product ROS concentrations without damaging the enzyme, making it particularly well suited for the modern surface ocean.

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An Iron-containing Superoxide Dismutase from Escherichia coli

Cited by 355 publications

References 29 publications

Structure and gene expression of theE. coliMn-superoxide dismutase gene

Structure and gene expression of theE. coliMn-superoxide dismutase gene

Exploring the microbial metalloproteome using MIRAGE

Inter‐domain horizontal gene transfer of nickel‐binding superoxide dismutase

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