ER stress-induced reactive oxygen species (ROS) are detrimental for the fitness of a thioredoxin reductase mutantCitation formats

  • External authors:
  • Paraskevi Kritsiligkou
  • Jonathan D. Rand
  • Alan Weids
  • Ximeng Wang

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ER stress-induced reactive oxygen species (ROS) are detrimental for the fitness of a thioredoxin reductase mutant. / Kritsiligkou, Paraskevi; Rand, Jonathan D.; Weids, Alan; Wang, Ximeng ; Kershaw, Christopher; Grant, Christopher.

In: Journal of Biological Chemistry, 2018.

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Kritsiligkou, Paraskevi ; Rand, Jonathan D. ; Weids, Alan ; Wang, Ximeng ; Kershaw, Christopher ; Grant, Christopher. / ER stress-induced reactive oxygen species (ROS) are detrimental for the fitness of a thioredoxin reductase mutant. In: Journal of Biological Chemistry. 2018.

Bibtex

@article{0e0a4a21d589412b80366435ac408fef,
title = "ER stress-induced reactive oxygen species (ROS) are detrimental for the fitness of a thioredoxin reductase mutant",
abstract = "The unfolded protein response (UPR) is constitutively active in yeast thioredoxin reductase mutants suggesting a link between cytoplasmic thiol redox control and ER oxidative protein folding. The unique oxidative environment of the ER lumen requires tight regulatory control and we show that the active UPR is dependent on the presence of oxidised thioredoxins, rather than arising due to a loss of thioredoxin function. Preventing activation of the UPR by deletion of HAC1, encoding the UPR transcription factor, rescues a number of thioredoxin reductase mutant phenotypes including slow growth, shortened longevity and oxidation of the cytoplasmic glutathione pool. This is because the constitutive UPR in a thioredoxin reductase mutant results in the generation of hydrogen peroxide. The oxidation of thioredoxins in a thioredoxin reductase mutant requires aerobic metabolism and the presence of the Tsa1 and Tsa2 peroxiredoxins indicating that a complete cytoplasmic thioredoxin system is crucial for maintaining ER redox homeostasis.",
keywords = "endoplasmic reticulum stress (ER stress), Peroxiredoxin, Thioredoxin, Thioredoxin, reactive oxygen species (ROS), redox regulation",
author = "Paraskevi Kritsiligkou and Rand, {Jonathan D.} and Alan Weids and Ximeng Wang and Christopher Kershaw and Christopher Grant",
year = "2018",
doi = "10.1074/jbc.RA118.001824",
language = "English",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",

}

RIS

TY - JOUR

T1 - ER stress-induced reactive oxygen species (ROS) are detrimental for the fitness of a thioredoxin reductase mutant

AU - Kritsiligkou, Paraskevi

AU - Rand, Jonathan D.

AU - Weids, Alan

AU - Wang, Ximeng

AU - Kershaw, Christopher

AU - Grant, Christopher

PY - 2018

Y1 - 2018

N2 - The unfolded protein response (UPR) is constitutively active in yeast thioredoxin reductase mutants suggesting a link between cytoplasmic thiol redox control and ER oxidative protein folding. The unique oxidative environment of the ER lumen requires tight regulatory control and we show that the active UPR is dependent on the presence of oxidised thioredoxins, rather than arising due to a loss of thioredoxin function. Preventing activation of the UPR by deletion of HAC1, encoding the UPR transcription factor, rescues a number of thioredoxin reductase mutant phenotypes including slow growth, shortened longevity and oxidation of the cytoplasmic glutathione pool. This is because the constitutive UPR in a thioredoxin reductase mutant results in the generation of hydrogen peroxide. The oxidation of thioredoxins in a thioredoxin reductase mutant requires aerobic metabolism and the presence of the Tsa1 and Tsa2 peroxiredoxins indicating that a complete cytoplasmic thioredoxin system is crucial for maintaining ER redox homeostasis.

AB - The unfolded protein response (UPR) is constitutively active in yeast thioredoxin reductase mutants suggesting a link between cytoplasmic thiol redox control and ER oxidative protein folding. The unique oxidative environment of the ER lumen requires tight regulatory control and we show that the active UPR is dependent on the presence of oxidised thioredoxins, rather than arising due to a loss of thioredoxin function. Preventing activation of the UPR by deletion of HAC1, encoding the UPR transcription factor, rescues a number of thioredoxin reductase mutant phenotypes including slow growth, shortened longevity and oxidation of the cytoplasmic glutathione pool. This is because the constitutive UPR in a thioredoxin reductase mutant results in the generation of hydrogen peroxide. The oxidation of thioredoxins in a thioredoxin reductase mutant requires aerobic metabolism and the presence of the Tsa1 and Tsa2 peroxiredoxins indicating that a complete cytoplasmic thioredoxin system is crucial for maintaining ER redox homeostasis.

KW - endoplasmic reticulum stress (ER stress)

KW - Peroxiredoxin

KW - Thioredoxin

KW - Thioredoxin, reactive oxygen species (ROS)

KW - redox regulation

U2 - 10.1074/jbc.RA118.001824

DO - 10.1074/jbc.RA118.001824

M3 - Article

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

ER -