Molecular cloning and characterization of a peroxiredoxin from Phanerochaete chrysosporium

Quan Jiang, Yong Hong Yan, Guo Ku Hu, Yi Zheng Zhang

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


Peroxiredoxins (Prxs) are a ubiquitous family of peroxidases widely distributed among prokaryotes and eukaryotes. Here, we report on the cloning and functional characterization of a cDNA designated PcPrx-1, encoding peroxiredoxin from the white-rot fungus Phanerochaete chrysosporium. The full-length PcPrx-1 cDNA (932 bp) contains an open reading frame of 200 amino acid residues with a molecular mass of 22.1 kDa. The deduced primary structure of PcPrx-1 polypeptide shows a high level of sequence identity to other recently identified 2-cys peroxiredoxins. The recombinant PcPrx-1 protein was expressed as a histidine fusion protein in Escherichia coli and purified with a Ni 2+-column. The purified protein was shown to have a protective effect against plasmid DNA cleavage by reactive oxygen species. The PcPrx-1 protein displays the ability to remove H2O2 in a ferrithiocyanate system. The results of this study suggest that PcPrx-1 may play a protective role against oxidative stress in P. chrysosporium.

Original languageEnglish (US)
Pages (from-to)659-668
Number of pages10
JournalCellular and Molecular Biology Letters
Issue number4
StatePublished - 2005
Externally publishedYes


  • Cloning
  • Expression
  • Peroxiredoxin
  • Phanerochaete chrysosporium

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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