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Integrative Dynamic proteomics and acyl-proteomics analyses in Clostridium butyricum

ABSTRACT: Clostridium butyricum is a notable butyrate-producing intestinal probiotic that has been utilized for the enhancement and treatment of various intestinal and extraintestinal diseases. Acetate and butyrate, as significant metabolites of this bacterium, are short-chain fatty acids (SCFAs) that play crucial roles in maintaining intestinal stability and safeguarding host health. However, the regulatory functions of lysine butyrylation (Kbu) and acetylation (Kac), mediated by these metabolites, remain inadequately understood. In this study, we performed a comprehensive dynamic multi-omic analysis encompassing protein expression, lysine acetylation, and butyrylation in C. butyricum. Our quantitative multi-omic analysis identified a total of 2,622 proteins, 1,887 Kbu sites, and 2,188 Kac sites. Subsequent bioinformatic analyses revealed that biological functions such as gene expression and energy metabolism, exhibited dynamic changes throughout the growth cycle at both the proteome and post-translational modification (PTM) levels. Enzymatic experiment indicated the specific butyrylation regulation in alanine-tRNA ligase, GMP synthase, and butyrate kinase. This study enhances the current understanding of lysine acylations in bacteria and focuses on elucidating the finely-tuned regulatory mechanisms of lysine butyrylation during the growth and development of C. butyricum.

ORGANISM(S): Clostridium Butyricum Dora_1

SUBMITTER: Junyu Xu

PROVIDER: PXD069757 | iProX | Tue Oct 21 00:00:00 BST 2025

REPOSITORIES: iProX

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