A 26 kDa protein of Helicobacter pylori shows alkyl hydroperoxide reductase (AhpC) activity and the mono-cistronic transcription of the gene is affected by pH

The 26 kDa protein of Helicobacter pylori, with 67% amino acid identity to alkyl hydroperoxide reductase (AhpC) of Campylobacter jejuni, was studied. We wanted to evaluate it the protein has AhpC activity. Therefore, an Escherichia coli mutant defective for alkyl hydroperoxide reductase and a plasmid expressing the 26 kDa protein from H. pylori were used in complementation studies. The complemented E. coli mutant showed a decreased sensitivity to cumene hydroperoxide indicating that the 26 kDa protein of H. pylori has AhpC activity and could be of importance in the defence against oxidative stress. Furthermore, Northern blot analysis detected one mRNA transcript of approximately 700 bp which is in agreement with the gene being transcribed as a single gene with its own promoter. This promoter region was further characterized by primer extension experiments. Additional studies on how environmental factors, such as long term growth and pH, can affect the transcription of the gene were performed on two H. pylori strains. We found that low pH and long term growth repressed transcription of the gene. Attempts to construct a mutant deficient for the gene in H. pylori were unsuccessful. (C) 2000 Academic Press.