Characterization of the peroxiredoxin 1 subfamily from Tetrahymena thermophila

Sarmad Al-Asadi, Arif Malik, Rigers Bakiu, Gianfranco Santovito, Ian Menz, Kathy Schuller

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


Peroxiredoxins are antioxidant enzymes that use redox active Cys residues to reduce H2O2 and various organic hydroperoxides to less reactive products, and thereby protect cells against oxidative stress. In yeasts and mammals, the Prx1 proteins are sensitive to hyperoxidation and consequent loss of their peroxidase activity whereas in most bacteria they are not. In this paper we report the characterization of the Prx1 family in the non-parasitic protist Tetrahymena thermophila. In this organism, four genes potentially encoding Prx1 have been identified. In particular, we show that the mitochondrial Prx1 protein (Prx1m) from T. thermophila is relatively robust to hyperoxidation. This is surprising given that T. thermophila is a eukaryote like yeasts and mammals. In addition, the proliferation of the T. thermophila cells was relatively robust to inhibition by H2O2, cumene hydroperoxide and plant natural products that are known to promote the production of H2O2. In the presence of these agents, the abundance of the T. thermophila Prx1m protein was shown to increase. This suggested that the Prx1m protein may be protecting the cells against oxidative stress. There was no evidence for any increase in Prx1m gene expression in the stressed cells. Thus, increasing protein stability rather than increasing gene expression may explain the increasing Prx1m protein abundance we observed.
Original languageEnglish
Pages (from-to)4745-4768
Number of pages24
JournalCellular and Molecular Life Sciences
Issue number23
Early online date25 May 2019
Publication statusPublished - Dec 2019


  • Alveolates
  • Ciliated protozoa
  • Antioxidant enzymes
  • Oxidative stress
  • Plant natural products

Cite this