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Cadmium Toxicity in Glutathione Mutants of Escherichia coli
- Source :
- Journal of Bacteriology. 190:5439-5454
- Publication Year :
- 2008
- Publisher :
- American Society for Microbiology, 2008.
-
Abstract
- The higher affinity of Cd 2+ for sulfur compounds than for nitrogen and oxygen led to the theoretical consideration that cadmium toxicity should result mainly from the binding of Cd 2+ to sulfide, thiol groups, and sulfur-rich complex compounds rather than from Cd 2+ replacement of transition-metal cations from nitrogen- or oxygen-rich biological compounds. This hypothesis was tested by using Escherichia coli for a global transcriptome analysis of cells synthesizing glutathione (GSH; wild type), γ-glutamylcysteine (Δ gshB mutant), or neither of the two cellular thiols (Δ gshA mutant). The resulting data, some of which were validated by quantitative reverse transcription-PCR, were sorted using the KEGG (Kyoto Encyclopedia of Genes and Genomes) orthology system, which groups genes hierarchically with respect to the cellular functions of their respective products. The main difference among the three strains concerned tryptophan biosynthesis, which was up-regulated in wild-type cells upon cadmium shock and strongly up-regulated in Δ gshA cells but repressed in Δ gshB cells containing γ-glutamylcysteine instead of GSH. Overall, however, all three E. coli strains responded to cadmium shock similarly, with the up-regulation of genes involved in protein, disulfide bond, and oxidative damage repair; cysteine and iron-sulfur cluster biosynthesis; the production of proteins containing sensitive iron-sulfur clusters; the storage of iron; and the detoxification of Cd 2+ by efflux. General energy conservation pathways and iron uptake were down-regulated. These findings indicated that the toxic action of Cd 2+ indeed results from the binding of the metal cation to sulfur, lending support to the hypothesis tested.
- Subjects :
- Physiology and Metabolism
Mutant
chemistry.chemical_element
Biology
medicine.disease_cause
Models, Biological
Microbiology
chemistry.chemical_compound
Biosynthesis
Genes, Reporter
Escherichia coli
medicine
Molecular Biology
Oligonucleotide Array Sequence Analysis
chemistry.chemical_classification
Cadmium
Reverse Transcriptase Polymerase Chain Reaction
Escherichia coli Proteins
Gene Expression Profiling
Wild type
Dipeptides
Glutathione
beta-Galactosidase
Adaptation, Physiological
Molecular biology
Artificial Gene Fusion
chemistry
Biochemistry
Thiol
Gene Deletion
Metabolic Networks and Pathways
Cysteine
Subjects
Details
- ISSN :
- 10985530 and 00219193
- Volume :
- 190
- Database :
- OpenAIRE
- Journal :
- Journal of Bacteriology
- Accession number :
- edsair.doi.dedup.....5145e9a936b9e9694764a5e2fc42e41e