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Status: Bibliographieeintrag

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Verfasst von:Gutscher, Marcus [VerfasserIn]   i
 Sobotta, Mirko Christoph [VerfasserIn]   i
 Wabnitz, Guido H. [VerfasserIn]   i
 Ballikaya, Seda [VerfasserIn]   i
 Meyer, Andreas [VerfasserIn]   i
 Samstag, Yvonne [VerfasserIn]   i
 Dick, Tobias P. [VerfasserIn]   i
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
 year:2009
 number:46
 pages:31532-31540
 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
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.
DOI:doi:10.1074/jbc.M109.059246
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: https://doi.org/10.1074/jbc.M109.059246
 Volltext: https://www.sciencedirect.com/science/article/pii/S0021925820378984
 DOI: https://doi.org/10.1074/jbc.M109.059246
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Disulfides
 Flow Cytometry
 Glutathione Peroxidase
 Green Fluorescent Proteins
 HeLa Cells
 Humans
 Hydrogen Peroxide
 Oxidants
 Oxidation-Reduction
 Phospholipid Hydroperoxide Glutathione Peroxidase
 Recombinant Fusion Proteins
 Saccharomyces cerevisiae
 Saccharomyces cerevisiae Proteins
 Sulfhydryl Compounds
 T-Lymphocytes
 Transcription Factors
K10plus-PPN:1763019152
Verknüpfungen:→ Zeitschrift

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