Global Profiling of Protein Phosphorylation, Acetylation, and β-Hydroxybutyrylation in .

Protein post-translational modifications (PTMs) regulate protein functions but remain poorly characterized in . This study examined three PTMs: lysine acetylation (Kac), lysine β-hydroxybutyrylation (Kbhb), and phosphorylation. Using LC-MS/MS, we identified 4571 Kac sites, 7812 Kbhb sites, and 6237 phosphorylation sites across 2455, 3109, and 2786 proteins, respectively.

Integration of Epigenome and Lactylome Reveals the Regulation of Lipid Production in .

Lysine lactylation (Kla) is a kind of novel post-translational modification (PTM) that participates in gene expression and various metabolic processes. has a remarkable capacity for triacylglycerol (TAG) production under nitrogen stress. To elucidate the involvement of lactylation in lipid synthesis, we conducted chromatin immunoprecipitation sequencing (ChIP-seq) and mRNA-seq analyses to monitor lactylation modifications and transcriptome alterations in .

Novel Insight of Nitrogen Deprivation Affected Lipid Accumulation by Genome-Wide Lactylation in .

Lysine lactylation (kla) as a post-translational modification (PTM) is linked to chromatin remodeling and gene transcription. Nitrogen stress can induce triacylglyceride (TAG) accumulation in most microalgae. To reveal lipid synthesis from another layer, the 4D label-free proteome method was used to track lactylation modifications and protein expression profiles after 3 days of nitrogen deprivation in to analyze the function and prevalence of lactylation.