Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli

We found that the Aop1 gene shows significant nucleotide sequence similarity to the gene coding for the C22 subunit of Salmonella typhimurium alkylhydroperoxide reductase, which is found in other bacteria, suggesting it functions as an antioxidant protein

K Tsuji; N G Copeland; N A Jenkins; M Obinata


Scholarcy highlights

  • The MER5 cDNA, which encoded a 257-amino-acid protein showing no sequence .identity with other known proteins, was cloned from RNA preferentially synthesized in murine erythroleukaemia cells during the early period of MEL cell differentiation
  • After we had published the results of that study, the sequence of a C22 subunit of bacterial alkylhydroperoxide reductase was reported and we found that the bacterial gene shows 38 % identity with the MER5 gene
  • In the present study we report that the MER5 gene can complement bacterial mutation and that its product is a new type of mammalian antioxidant protein
  • Salmonella alkylhydroperoxide reductase consists of two subunits, C22 and F52a; F52a shows strong sequence similarity to thioredoxin reductase
  • The sequence similarity between the Salmonella C22 subunit and the MER5 product was 38.0%, and noteworthy that the archaebacterium C22 homologue is linked to the superoxide dismutase gene rather than thioredoxin reductase gene
  • The resistance to H202 was especially high. These results indicate that the MERS gene product can complement the activity of the C22 subunit of bacterial alkylhydroperoxide reductase
  • The AopJ gene products may be a new type of protein involved in regulation of proliferation/differentiation and antioxidant functions through redox regulation in mammalian cells

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