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Exploring the microbiome-wide lysine acetylation, succinylation and propionylation in human gut microbiota

By Xu Zhang, Kai Cheng, Zhibin Ning, Janice Mayne, Krystal Walker, Hao Chi, Charles Farnsworth, Kimberly Lee, Daniel Figeys

Posted 14 Dec 2020
bioRxiv DOI: 10.1101/2020.12.14.422746

Lysine acylations are important post-translational modifications that are present in both eukaryotes and prokaryotes, regulating diverse cellular functions. Our knowledge of the microbiome lysine acylation remains limited due to the lack of efficient analytical and bioinformatics methods for complex microbial communities. We show that serial enrichment using motif antibodies successfully captures peptides containing lysine acetylation, propionylation and succinylation from human gut microbiome samples. A new bioinformatic workflow consisting of unrestricted database search confidently identified >60,000 acetylated, and ~20,000 propionylated and succinylated gut microbial peptides. Characterization of these identified modification-specific metaproteomes, i.e. meta-PTMomes, demonstrates that lysine acylations are differentially distributed in microbial species with different metabolic capabilities. This study provides an analytical framework, consisting of a serial immunoaffinity enrichment and an open database search strategy, for the study of lysine acylations in microbiome, which enables functional microbiome studies at the post-translational level.

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