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SILAC based quantitative 3-hydroxybutyromics of HBO1-WT and HBO1-KO HeLa cells

ABSTRACT: Ketogenesis derived BHB facilitates 3-hydroxybutyrylation on lysine linking metabolism with epigenetic regulation. Herein, we found HBO1 served as 3-hydroxybutyryltransferase preferentially catalyzing lysine 9 of histone H3 (H3K9bhb). Moreover, total 1171 Kbhb sites on 582 proteins were identified. Collectively, we firstly descibed HBO1 mediated Kbhb regulatory network in HeLa cells.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell Of Cervix, Hela Cell

DISEASE(S): Cervical Cancer

SUBMITTER: siyu wang

LAB HEAD: Kai Zhang

PROVIDER: PXD051668 | Pride | 2025-07-04

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	HBO1_Histone_kbhb.raw	Raw
	HBO1_cytoplasm_Kbhb.raw	Raw
	Histone-Kbhb-Sites.txt	Txt
	Histone-proteomics-1.raw	Raw
	Histone-proteomics-2.raw	Raw

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Project description:Characterization of the lysine β-hydroxybutyrylome, proteome-wide, will start to define its cellular targets and enable investigation of its impact under ketogenesis. Here, we show the induction of global protein Kbhb in the liver. We identified 891 sites of Kbhb within 267 proteins belonging to macronutrient, detoxification and 1-carbon metabolic pathways, among others, in starved liver.

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Quantitative Proteomics Analysis Expands the Roles of Lysine -Hydroxybutyrylation Pathway in Response to Environmental β-Hydroxybutyrate

Project description:Lysine -hydroxybutyrylation (Kbhb) is a newly identified protein post-translational modification that derived from the ketone body β-hydroxybutyrate (BHB). BHB is synthesized in the liver from fatty acids and could be delivered to peripheral tissues when the supply of glucose is too low for the body’s energetic needs. The plasma concentration of BHB can increase up to 20 mM during starvation and in pathological conditions. Despite the progresses, how the cells that do not produce BHB respond to elevated environmental BHB remains largely unknown. Given that BHB significantly drives Kbhb, here we performed a quantitative proteomics study to characterize the BHB-induced lysine -hydroxybutyrylome and acetylome. A total of 840 unique Kbhb sites across 429 proteins were identified, with 42 sites from 39 proteins being increased by more than 50% in response to BHB. The upregulated β-hydroxybutyrylome induced by BHB are involved in aminoacyl-tRNA biosynthesis, 2-oxocarboxylic acid metabolism, citrate cycle (TCA cycle), glycolysis/gluconeogenesis, and pyruvate metabolism pathways. Moreover, some BHB-targeted Kbhb substrates are potentially linked to diseases such as cancer. Taken together, this study revealed the dynamics of lysine -hydroxybutyrylome and acetylome in response to environmental BHB, which sheds light on the roles for Khib in regulation of diverse cellular processes and provides new insights into the biological functions of BHB.

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