Thioredoxin or glutaredoxin in Escherichia coli is essential for sulfate reduction but not for deoxyribonucleotide synthesis.

Abstract excerpt

We have shown previously that Escherichia coli cells constructed to lack both thioredoxin and glutaredoxin are not viable unless they also acquire an additional mutation, which we called X. Here we show that X is a cysA mutation. Our data suggest that the inviability of a trxA grx double mutant is due to the accumulation of 3'-phosphoadenosine 5'-phosphosulfate (PAPS), an intermediate in the sulfate assimilation...

Topics

• Adenine Nucleotides
• Bacterial Proteins
• Cystine
• Deoxyribonucleotides
• Escherichia coli
• Genotype
• Glutaredoxins
• Mutation
• Oxidation-Reduction
• Oxidoreductases
• Phosphoadenosine Phosphosulfate