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. 2023 Mar 28;13:5029. doi: 10.1038/s41598-023-31900-5

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© The Author(s) 2023

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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Computational modeling and mass spectrometry analysis revealed the mechanism of lysine acylation on CoA-binding protein within the mitochondria. (a) Schematic diagram of the experimental approaches in this study and the hypotheses tested. Statistical analyses of proteome-wide MS acylation datasets using database annotation data, and subsequent structural modeling of acylated proteins, generated a proposed mechanism for CoA-binding-protein hyperacylation. This mechanism was validated by in-vitro MS analysis of a reported acylated protein.