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- W3113098651 abstract "Abstract Background 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. Results 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. Conclusion 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." @default.
- W3113098651 created "2020-12-21" @default.
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- W3113098651 date "2020-12-14" @default.
- W3113098651 modified "2023-09-27" @default.
- W3113098651 title "Exploring the microbiome-wide lysine acetylation, succinylation and propionylation in human gut microbiota" @default.
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- W3113098651 doi "https://doi.org/10.1101/2020.12.14.422746" @default.
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