Article
Redox requirements for ubiquitin-like urmylation of Ahp1, a 2-Cys peroxiredoxin from yeast.
Redox biology - 1 Feb 2020
Brachmann Cindy, Kaduhr Lars, Jüdes André, Ravichandran Keerthiraju Ethiraju, West James D, Glatt Sebastian, Schaffrath Raffael
Abstract excerpt
The yeast peroxiredoxin Ahp1, like related anti-oxidant enzymes in other species, undergoes urmylation, a lysine-directed conjugation to ubiquitin-like modifier Urm1. Ahp1 assembles into a homodimer that detoxifies peroxides via forming intersubunit disulfides between peroxidatic and resolving cysteines that are subsequently reduced by the thioredoxin system. Although urmylation coincides with oxidative stress,...
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