Widespread protein lysine acetylation in gut microbiome and its alterations in patients with Crohn’s disease

Zhang, Xu, Ning, Zhibin, Mayne, Janice, Yang, Yidai, Deeke, Shelley A., Walker, Krystal, Farnsworth, Charles L., Stokes, Matthew P., Couture, Jean François, Mack, David, Stintzi, Alain and Figeys, Daniel (2020) Widespread protein lysine acetylation in gut microbiome and its alterations in patients with Crohn’s disease. Nature Communications, 11 (1). ISSN 2041-1723

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Abstract

Lysine acetylation (Kac), an abundant post-translational modification (PTM) in prokaryotes, regulates various microbial metabolic pathways. However, no studies have examined protein Kac at the microbiome level, and it remains unknown whether Kac level is altered in patient microbiomes. Herein, we use a peptide immuno-affinity enrichment strategy coupled with mass spectrometry to characterize protein Kac in the microbiome, which successfully identifies 35,200 Kac peptides from microbial or human proteins in gut microbiome samples. We demonstrate that Kac is widely distributed in gut microbial metabolic pathways, including anaerobic fermentation to generate short-chain fatty acids. Applying to the analyses of microbiomes of patients with Crohn’s disease identifies 52 host and 136 microbial protein Kac sites that are differentially abundant in disease versus controls. This microbiome-wide acetylomic approach aids in advancing functional microbiome research.

Item Type: Article
Additional Information: Publisher Copyright: © 2020, The Author(s).
Uncontrolled Keywords: chemistry(all),biochemistry, genetics and molecular biology(all),general,physics and astronomy(all),sdg 3 - good health and well-being ,/dk/atira/pure/subjectarea/asjc/1600
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
UEA Research Groups: Faculty of Medicine and Health Sciences > Research Centres > Metabolic Health
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Depositing User: LivePure Connector
Date Deposited: 26 Mar 2026 12:30
Last Modified: 26 Mar 2026 12:30
URI: https://ueaeprints.uea.ac.uk/id/eprint/102595
DOI: 10.1038/s41467-020-17916-9

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