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. 2024 Jun 25;15:5360. doi: 10.1038/s41467-024-49489-2

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — A Cysteamine dioxygenase (ADO) can catalyse the oxidation of the N-terminal cysteine (Nt-Cys) of a target protein, incorporating two oxygen atoms from molecular oxygen^13,49. This allows the protein to be recognised and so degraded by the Arg/N-degron pathway⁵⁰. ADO-catalysed Nt-Cys oxidation is significantly reduced in hypoxia. B N-terminal acetyltransferase enzymes (NATs) catalyse the acetylation of the N-terminal residue of a target protein, involving the transfer of an acetyl group from acetyl coenzyme A to the N-terminal amine. This can have a range of effects including stabilisation of the target protein, enhanced binding and degradation by the acetyl branch of the N-degron pathway²⁴. Created using Biorender (license agreement #YB26TL2XO9).