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Preparation and Reactions of Thiols02:33

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Updated: Oct 18, 2025

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
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Acetylated Thioredoxin Reductase 1 Resists Oxidative Inactivation.

David E Wright1, Nikolaus Panaseiko1, Patrick O'Donoghue1,2

  • 1Departments of Biochemistry, The University of Western Ontario, London, ON, Canada.

Frontiers in Chemistry
|October 4, 2021
PubMed
Summary

Acetylation protects Thioredoxin Reductase 1 (TrxR1) from oxidative damage. Both specific and general acetylation enhance TrxR1

Keywords:
acetylationenzymologygenetic code expansionoxidationpost-translational modificationredox biologyselenocysteine

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Thioredoxin Reductase 1 (TrxR1) is crucial for cellular defense against oxidative stress and chemotherapy-induced damage.
  • Acetylation of TrxR1 is linked to oxidative stress, but its functional role under oxidizing conditions remains unclear.
  • Selenocysteine is vital for TrxR1 enzymatic activity.

Purpose of the Study:

  • To investigate the functional consequences of TrxR1 acetylation under oxidative stress.
  • To compare the effects of site-specific versus non-specific acetylation on TrxR1 stability and activity.
  • To elucidate the regulatory mechanisms of TrxR1 in response to oxidative conditions.

Main Methods:

  • Genetic code expansion was employed to create recombinant, site-specifically acetylated TrxR1 variants containing selenocysteine.
  • Enzymological assays were performed to assess TrxR1 activity, oxidative inactivation, and multimer formation.
  • Non-specific acetylation of TrxR1 was induced using aspirin, followed by mass spectrometry analysis.

Main Results:

  • Site-specific acetylation at lysine residues enhances TrxR1 activity by modulating dimer and tetramer formation.
  • Acetylated TrxR1 exhibits resistance to oxidative inactivation and peroxide-induced multimerization.
  • Non-specifically acetylated TrxR1 demonstrates sustained activity under strongly oxidizing conditions, unlike unmodified TrxR1.

Conclusions:

  • Both site-specific and general acetylation serve as regulatory mechanisms for TrxR1.
  • Acetylation enhances TrxR1's resilience to oxidative damage, preserving its protective cellular functions.
  • These findings offer insights into managing oxidative stress in cellular defense and therapeutic contexts.