N-terminal cysteine acetylation and oxidation patterns may define protein stability.

ABSTRACT: Oxygen homeostasis is maintained in plants and animals by O₂-sensing enzymes initiating adaptive responses to low O₂ (hypoxia). Recently, the O₂-sensitive enzyme ADO was shown to initiate degradation of target proteins RGS4/5 and IL32 via the Cysteine/Arginine N-degron pathway. ADO functions by catalysing oxidation of N-terminal cysteine residues, but despite multiple proteins in the human proteome having an N-terminal cysteine, other endogenous ADO substrates have not yet been identified. This could be because alternative modifications of N-terminal cysteine residues, including acetylation, prevent ADO-catalysed oxidation. Here we investigate the relationship between ADO-catalysed oxidation and NatA-catalysed acetylation of a broad range of protein sequenc

SUBMITTER: Heathcote KC 

PROVIDER: S-EPMC11199558 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature