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Cited by 114Redox biology and oxidative stressPlant Stress Responses and TolerancePhotosynthetic Processes and Mechanisms

Isolation and characterization of a thioredoxin‐dependent peroxidase from Chlamydomonas reinhardtii

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Goyer, Aymeric, Haslekås, Camilla, Miginiac‐Maslow, Myroslawa, Klein, Uwe, Le Marechal, Pierre, Jacquot, Jean‐Pierre, Decottignies, Paulette·2002·European Journal of Biochemistry
DOI 10.1046/j.0014-2956.2001.02648.x
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Abstract

All living organisms contain redox systems involving thioredoxins (Trx), proteins featuring an extremely conserved and reactive active site that perform thiol-disulfide interchanges with disulfide bridges of target proteins. In photosynthetic organisms, numerous isoforms of Trx coexist, as revealed by sequencing of Arabidopsis genome. The specific functions of many of them are still unknown. In an attempt to find new molecular targets of Trx in Chlamydomonas reinhardtii, an affinity column carrying a cytosolic Trx h mutated at the less reactive cysteine of its active site was used to trap Chlamydomonas proteins that form mixed disulfides with Trx. The major protein bound to the column was identified by amino-acid sequencing and mass spectrometry as a thioredoxin-dependent 2Cys peroxidase. Isolation and sequencing of its gene revealed that this peroxidase is most likely a chloroplast protein with a high homology to plant 2Cys peroxiredoxins. It is shown that the Chlamydomonas peroxiredoxin (Ch-Prx1) is active with various thioredoxin isoforms, functions as an antioxidant toward reactive oxygen species (ROS), and protects DNA against ROS-induced degradation. Expression of the peroxidase gene in Chlamydomonas was found to be regulated by light, oxygen concentration, and redox state. The data suggest a role for the Chlamydomonas Prx in ROS detoxification in the chloroplast.

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  • 2-Cys peroxiredoxin is active with various thioredoxin isoforms and functions as an antioxidant toward reactive oxygen species in C. reinhardtii.

    “It has been shown that 2-Cys peroxiredoxin is active with various thioredoxin isoforms and functions as an antioxidant toward reactive oxygen species in C. reinhardtii (Goyer et al., 2002).”

    From Responses of<i>Nannochloropsis oceanica</i>IMET1 to Long-Term Nitrogen Starvation and Recovery (2013) · cites this paper as Goyer et al., 2002

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Research works printed but not linked: 2

  1. Chae, H.Z., Robison, K., Poole, L.B., Church, G., Storz, G. & Rhee, S.G. (1994) Cloning and sequencing of thiol-speci®c antioxidant from mammalian brain: alkyl reductases and thiol- speci®c antioxidant de®ne a large family of antioxidant enzymes. Proc. Natl Acad. Sci. USA 91, 7022±7026.
  2. Lemaire, S. (1999) Etude structurale et fonctionnelle des systeÁ mes ferre doxine et thiore doxine de pendants chez Chlamy- domonas Reinhardtii. PhD thesis. UniversiteÁ Paris XI, Orsay, France.

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Authors
Goyer, A., Haslekås, C., Miginiac‐Maslow, M., Klein, U., Le Marechal, P., Jacquot, J., & Decottignies, P.
Affiliations
  • Université Paris-Sud (FR)
  • University of Oslo (NO)
  • Interactions Arbres-Microorganismes (FR)
ORCID
Venue
European Journal of Biochemistry
Publisher
Wiley
Published
2002-01
Volume
269
Issue
1
Pages
272-282
ISSN
  • 0014-2956 (ISSN-L)
  • 1432-1033
DOI
10.1046/j.0014-2956.2001.02648.x
OpenAlex
W1596005526
Cited by
114
References
42
Citations by year
2025: 2 · 2024: 3 · 2023: 3 · 2021: 3 · 2020: 1 · 2019: 4 · 2018: 5 · 2017: 5 · 2016: 4 · 2015: 2 · 2014: 3 · 2013: 5 · 2012: 3
FWCI
4.51
Type
journal article
Language
en
Open access
Licence
onlinelibrary.wiley.com/termsAndConditions#vor (vor, 667 d)
Locations
  • European Journal of Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Stress Responses and Tolerance
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
Keywords
Chlamydomonas reinhardtii, thioredoxin, mixed disulfide formation, chloroplast proteins, reactive oxygen species scavenging, antioxidant activity, DNA protection, gene expression regulation, redox state, light regulation, oxygen concentration
MeSH terms
Amino Acid Sequence, Animals, Cloning, Molecular, Gene Expression Regulation, Molecular Sequence Data, Peroxidases, Recombinant Proteins, Chlamydomonas reinhardtii, DNA, Complementary, Oxidative Stress, Peroxiredoxins

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