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Lysine Methylpropionylation, a Hybrid Post-Translational Modification Mediated by p300/PCAF Couples Metabolic Dynamics with Protein Function

ABSTRACT: Lysine Methylpropionylation, a Hybrid Post-Translational Modification Mediated by p300/PCAF Couples Metabolic Dynamics with Protein Function

PROVIDER: PRJNA1252466 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR33209816_1.fastq.gz	Fastqsanger.gz
	SRR33209816_2.fastq.gz	Fastqsanger.gz
	SRR33209817_1.fastq.gz	Fastqsanger.gz
	SRR33209817_2.fastq.gz	Fastqsanger.gz
	SRR33209818_1.fastq.gz	Fastqsanger.gz

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Lysine Methylpropionylation, a Hybrid Post-Translational Modification Mediated by p300/PCAF Couples Metabolic Dynamics with Protein Function

Project description:Lysine alkylation and acylation serve as crucial links between cellular metabolism and a wide range of biological functions. However, hybrid modifications that combine features of both alkylation and acylation remain largely unexplored. Here, we report the discovery and in-depth characterization of lysine methylpropionylation (Kpm), a hybrid post-translational modification (PTM) defined by the propionylation of monomethyllysine residues. Genome-wide chromatin immunoprecipitation coupled with transcriptomic profiling revealed that Kpm exhibits distinct genomic distribution compared to canonical Kac and Kpr, with preferential enrichment at promoters of genes involved in metabolic pathways. Together, our findings establish Kpm as a dual-feature PTM that integrates metabolic cues with both chromatin regulation and non-histone protein function, offering a mechanistic framework for understanding metabolism-proteome crosstalk.

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Project description:Post-translational modifications (PTMs) serve as critical regulatory mechanisms connecting metabolism and protein functions. Following our prior discovery of lysine lactylation (Kla), we herein report the identification and characterization of lysine pyruvylation (Kpy), a previously undescribed PTM driven by the central glycolytic hub metabolite pyruvate. Through integrated biochemical and proteomic strategies, we established the existence and specificity of Kpy. Proteomic profiling revealed Kpy sites across both histones and non-histone proteins, implicating its broad physiological significance. Notably, our investigations demonstrated that Kpy abundance fluctuates in respond to alterations in glycolytic flux and pyruvate concentration, providing a direct mechanism by which metabolic alterations influence protein functions. Additionally, we identified Sirtuin 3 (SIRT3) as the "eraser" enzyme for Kpy removal, while Histone acetyltransferase 1 (HAT1) and p300 (EP300) function as "writer" enzymes responsible for Kpy deposition. Initial mechanistic studies suggested Kpy's regulatory role in transcriptional control. Together, the elucidation of Kpy expands our understanding of metabolite-protein crosstalk through PTMs, providing mechanistic insights into pathophysiological processes and facilitating the development of targeted therapeutic interventions for metabolic disorders.

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