ArticleFrontiers in microbiology2026
Lysine acetylome profiling reveals a dual regulatory role in carbon flux redirection and RNA degradation inhibition in
Article in Frontiers in microbiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Introduction: Methods: In this study, we cultured Results: LC-MS/MS revealed 182 acetylated proteins and 398 sites exclusively in Sauton-medium-cultured strains; whereas 57 acetylated proteins and 141 sites were identified exclusively in nutrient-rich 7H9-medium-cultured strains. Additionally, 302 proteins and 462 sites were differentially acetylated between the Sauton- and 7H9-medium-cultured samples. Our bioinformatics analysis identified differences in whole-protein acetylation modifications in Discussion: Under the nutrient-limited conditions of Sauton medium culture, multiple sites within isocitrate dehydrogenase exhibited acetylation, leading to reduced enzyme activity. This effect may redirect a greater proportion of carbon flux towards the glyoxylate pathway. Conversely, in 7H9 medium, acetylation at residues K189 and K331 of isocitrate lyase may diminish enzyme activity, thereby channeling increased carbon flux towards the TCA cycle. Acetylation at 3-hydroxyacyl-CoA dehydrogenase (K370) and tryptophan-tRNA synthetase (K200) may reduce fatty acid and protein synthesis, thereby preventing excessive energy expenditure; acetylation at Oligoribonuclease K153 likely diminishes enzyme activity, thereby allowing
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