Proximity-based protein thiol oxidation by H2O2-scavenging peroxidases

• Verfasst von: Gutscher, Marcus [VerfasserIn]
• Verfasst von: Sobotta, Mirko Christoph [VerfasserIn]
• Verfasst von: Wabnitz, Guido H. [VerfasserIn]
• Verfasst von: Ballikaya, Seda [VerfasserIn]
• Verfasst von: Meyer, Andreas [VerfasserIn]
• Verfasst von: Samstag, Yvonne [VerfasserIn]
• Verfasst von: Dick, Tobias P. [VerfasserIn]
• Titel: Proximity-based protein thiol oxidation by H2O2-scavenging peroxidases
• Verf.angabe: Marcus Gutscher, Mirko C. Sobotta, Guido H. Wabnitz, Seda Ballikaya, Andreas J. Meyer, Yvonne Samstag, and Tobias P. Dick
• Jahr: 2009
• Umfang: 9 S.
• Teil: volume:284
• Teil: year:2009
• Teil: number:46
• Teil: pages:31532-31540
• Teil: extent:9
• Fussnoten: Im Titel ist die "2" jeweils tiefgestellt ; Elektronische Reproduktion der Druck-Ausgabe ; Gesehen am 16.07.2021
• Titel Quelle: Enthalten in: The journal of biological chemistry
• Ort Quelle: Bethesda, Md. : ASBMB Publications, 1905
• Jahr Quelle: 2009
• Band/Heft Quelle: 284(2009), 46, Seite 31532-31540
• ISSN Quelle: 1083-351X
• DOI: doi:10.1074/jbc.M109.059246
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Disulfides
• Sach-SW: Flow Cytometry
• Sach-SW: Glutathione Peroxidase
• Sach-SW: Green Fluorescent Proteins
• Sach-SW: HeLa Cells
• Sach-SW: Humans
• Sach-SW: Hydrogen Peroxide
• Sach-SW: Oxidants
• Sach-SW: Oxidation-Reduction
• Sach-SW: Phospholipid Hydroperoxide Glutathione Peroxidase
• Sach-SW: Recombinant Fusion Proteins
• Sach-SW: Saccharomyces cerevisiae
• Sach-SW: Saccharomyces cerevisiae Proteins
• Sach-SW: Sulfhydryl Compounds
• Sach-SW: T-Lymphocytes
• Sach-SW: Transcription Factors
• K10plus-PPN: 1763019152

Abstract

H(2)O(2) acts as a signaling molecule by oxidizing critical thiol groups on redox-regulated target proteins. To explain the efficiency and selectivity of H(2)O(2)-based signaling, it has been proposed that oxidation of target proteins may be facilitated by H(2)O(2)-scavenging peroxidases. Recently, a peroxidase-based protein oxidation relay has been identified in yeast, namely the oxidation of the transcription factor Yap1 by the peroxidase Orp1. It has remained unclear whether the protein oxidase function of Orp1 is a singular adaptation or whether it may represent a more general principle. Here we show that Orp1 is in fact not restricted to oxidizing Yap1 but can also form a highly efficient redox relay with the oxidant target protein roGFP (redox-sensitive green fluorescent protein) in mammalian cells. Orp1 mediates near quantitative oxidation of roGFP2 by H(2)O(2), and the Orp1-roGFP2 redox relay effectively converts physiological H(2)O(2) signals into measurable fluorescent signals in living cells. Furthermore, the oxidant relay phenomenon is not restricted to Orp1 as the mammalian peroxidase Gpx4 also mediates oxidation of proximal roGFP2 in living cells. Together, these findings support the concept that certain peroxidases harbor an intrinsic and powerful capacity to act as H(2)O(2)-dependent protein thiol oxidases when they are recruited into proximity of oxidizable target proteins.