A curious case of cysteines in human peroxiredoxin I.
Catalytic residues
Chaperone activity
Human peroxiredoxins
Redox stress
Saccharomyces cerevisiae
Yeast
Journal
Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639
Informations de publication
Date de publication:
10 2020
10 2020
Historique:
received:
06
08
2020
revised:
08
09
2020
accepted:
19
09
2020
pubmed:
5
10
2020
medline:
22
6
2021
entrez:
4
10
2020
Statut:
ppublish
Résumé
Peroxiredoxins (Prxs) are antioxidant proteins that are involved in cellular defence against reactive oxygen species and reactive nitrogen species. Humans have six peroxiredoxins, hPrxI-VI, out of which hPrxI and hPrxII belongs to the typical 2-Cys class sharing 90% conservation in their amino acid sequence including catalytic residues required to carry out their peroxidase and chaperone activities. Despite the high conservation between hPrxI and hPrxII, hPrxI behaves differently from hPrxII in its peroxidase and chaperone activity. We recently showed in yeast that in the absence of Tsa1 and Tsa2 (orthologs of hPrx) hPrxI protects the cells against different stressors whereas hPrxII does not. To understand this difference, we expressed catalytic mutants of hPrxI in yeast cells lacking the orthologs of hPrxI/II. We found that the catalytic mutants lacking peroxidase function including hPrxI
Identifiants
pubmed: 33011678
pii: S2213-2317(20)30943-5
doi: 10.1016/j.redox.2020.101738
pmc: PMC7530344
pii:
doi:
Substances chimiques
Hydrogen Peroxide
BBX060AN9V
Peroxidases
EC 1.11.1.-
Peroxiredoxins
EC 1.11.1.15
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
101738Informations de copyright
Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.
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