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Titel: Tsa1 is the dominant peroxide scavenger and a source of H2O2-dependent GSSG production in yeast
VerfasserIn: Zimmermann, Jannik UdsID
Lang, Lukas
Calabrese, Gaetano
Laporte, Hugo
Amponsah, Prince S.
Michalk, Christoph
Sukmann, Tobias
Oestreicher, Julian UdsID
Tursch, Anja
Peker, Esra
Owusu, Theresa N. E.
Weith, Matthias
Roma, Leticia Prates
Deponte, Marcel
Riemer, Jan
Morgan, Bruce UdsID
Sprache: Englisch
In:
Titel: Free Radical Biology & Medicine
Bandnummer: 226 (2025)
Seiten: 408-420
Verlag/Plattform: Elsevier
Erscheinungsjahr: 2024
Freie Schlagwörter: roGFP2
HyPer7
Peroxiredoxin
Catalase
Thiol peroxidase
Heme peroxidase
H2O2 scavenging
DDC-Sachgruppe: 500 Naturwissenschaften
Dokumenttyp: Journalartikel / Zeitschriftenartikel
Abstract: Hydrogen peroxide (H2O2) is an important biological molecule, functioning both as a second messenger in cell signaling and, especially at higher concentrations, as a cause of cell damage. Cells harbor multiple enzymes that have peroxide reducing activity in vitro. However, the contribution of each of these enzymes towards peroxide scavenging in vivo is less clear. Therefore, to directly investigate in vivo peroxide scavenging, we used the genetically encoded peroxide probes, roGFP2-Tsa2ΔCR and HyPer7, to systematically screen the peroxide scavenging capacity of baker’s yeast thiol and heme peroxidase mutants. We show that the 2-Cys peroxiredoxin Tsa1 alone is responsible for almost all exogenous H2O2 and tert-butyl hydroperoxide scavenging. Furthermore, Tsa1 can become an important source of H2O2-dependent cytosolic glutathione disulfide production. The two catalases and cytochrome c peroxidase only produce observable scavenging defects at higher H2O2 concentrations when these three heme peroxidases are removed in combination. We also analyzed the reduction of Tsa1 in vitro, revealing that the enzyme is efficiently reduced by thioredoxin-1 with a rate constant of 2.8 × 106 M− 1 s − 1 but not by glutaredoxin-2. Tsa1 reduction by reduced glutathione occurs nonenzymatically with a rate constant of 2.9 M− 1 s − 1 . Hence, the observed Tsa1-dependent glutathione disulfide production in yeast probably requires the oxidation of thioredoxins. Our findings clarify the importance of the various thiol and heme peroxidases for peroxide removal and suggest that most thiol peroxidases have alternative or specialized functions in specific subcellular compartments.
DOI der Erstveröffentlichung: 10.1016/j.freeradbiomed.2024.11.004
URL der Erstveröffentlichung: https://doi.org/10.1016/j.freeradbiomed.2024.11.004
Link zu diesem Datensatz: urn:nbn:de:bsz:291--ds-442681
hdl:20.500.11880/39563
http://dx.doi.org/10.22028/D291-44268
ISSN: 0891-5849
Datum des Eintrags: 4-Feb-2025
Bezeichnung des in Beziehung stehenden Objekts: Supplementary data
In Beziehung stehendes Objekt: https://ars.els-cdn.com/content/image/1-s2.0-S0891584924010268-mmc1.docx
https://ars.els-cdn.com/content/image/1-s2.0-S0891584924010268-mmc2.xlsx
Fakultät: M - Medizinische Fakultät
NT - Naturwissenschaftlich- Technische Fakultät
Fachrichtung: M - Biophysik
NT - Biowissenschaften
Professur: M - Jun.-Prof. Dr. Leticia Prates Roma
NT - Prof. Dr. Bruce Morgan
Sammlung:SciDok - Der Wissenschaftsserver der Universität des Saarlandes



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