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Redox requirements for ubiquitin-like urmylation of Ahp1, a 2-Cys peroxiredoxin from yeast.
- Source :
-
Redox biology [Redox Biol] 2020 Feb; Vol. 30, pp. 101438. Date of Electronic Publication: 2020 Jan 22. - Publication Year :
- 2020
-
Abstract
- The yeast peroxiredoxin Ahp1, like related anti-oxidant enzymes in other species, undergoes urmylation, a lysine-directed conjugation to ubiquitin-like modifier Urm1. Ahp1 assembles into a homodimer that detoxifies peroxides via forming intersubunit disulfides between peroxidatic and resolving cysteines that are subsequently reduced by the thioredoxin system. Although urmylation coincides with oxidative stress, it is unclear how this modification happens on a molecular level and whether it affects peroxiredoxin activity. Here, we report that thioredoxin mutants decrease Ahp1 urmylation in yeast and each subunit of the oxidized Ahp1 dimer is modified by Urm1 suggesting coupling of urmylation to dimerization. Consistently, Ahp1 mutants unable to form dimers, fail to be urmylated as do mutants that lack the peroxidatic cysteine. Moreover, Ahp1 urmylation involves at least two lysine residues close to the catalytic cysteines and can be prevented in yeast cells exposed to high organic peroxide concentrations. Our results elucidate redox requirements and molecular determinants critical for Ahp1 urmylation, thus providing insights into a potential link between oxidant defense and Urm1 utilization in cells.<br />Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.<br /> (Copyright © 2020 The Authors. Published by Elsevier B.V. All rights reserved.)
- Subjects :
- Catalytic Domain
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Fungal
Models, Molecular
Oxidation-Reduction
Peroxides metabolism
Peroxiredoxins chemistry
Peroxiredoxins genetics
Protein Conformation
Protein Multimerization
Saccharomyces cerevisiae genetics
Mutation
Peroxiredoxins metabolism
Saccharomyces cerevisiae enzymology
Saccharomyces cerevisiae Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2213-2317
- Volume :
- 30
- Database :
- MEDLINE
- Journal :
- Redox biology
- Publication Type :
- Academic Journal
- Accession number :
- 32004955
- Full Text :
- https://doi.org/10.1016/j.redox.2020.101438