ArticleThe Journal of biological chemistry2020
Activity of the yeast cytoplasmic Hsp70 nucleotide-exchange factor Fes1 is regulated by reversible methionine oxidation.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Black Tea Aqueous Extract Extends Yeast Longevity via Antioxidant Gene Activation: Transcriptomic Analysis of Anti-Aging Mechanisms.Food science & nutrition · 2025Article
- Ndufaf2, a protein in mitochondrial complex I, interactsRedox report : communications in free radical research · 2023Article
- Methionine Sulfoxide Reductases Suppress the Formation of the [Antioxidants (Basel, Switzerland) · 2023Article
- Proteolysis Degree of Protein Corona Affect Ultrasound-Induced Sublethal Effects onFoods (Basel, Switzerland) · 2022Article
- Profiling Dopamine-Induced Oxidized Proteoforms of β-synuclein by Top-Down Mass Spectrometry.Antioxidants (Basel, Switzerland) · 2021Article
- Structure and Electron-Transfer Pathway of the Human Methionine Sulfoxide Reductase MsrB3.Antioxidants & redox signaling · 2020Article
- Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase.Antioxidants (Basel, Switzerland) · 2020Article
- Top-Down Characterization of an Antimicrobial Sanitizer, Leading From Quenchers of Efficacy to Mode of Action.Frontiers in microbiology · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cells employ a vast network of regulatory pathways to manage intracellular levels of reactive oxygen species (ROS). An effectual means used by cells to control these regulatory systems are sulfur-based redox switches, which consist of protein cysteine or methionine residues that become transiently oxidized when intracellular ROS levels increase. Here, we describe a methionine-based oxidation event involving the yeast cytoplasmic Hsp70 co-chaperone Fes1. We show that Fes1 undergoes reversible methionine oxidation during excessively-oxidizing cellular conditions, and we map the site of this oxidation to a cluster of three methionine residues in the Fes1 core domain. Making use of recombinant proteins and a variety of
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Registered trials
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