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SILAC experiment quantifying the proteomics of WT and HBO1-KO HeLa

ABSTRACT: Lysine lactylation (Kla) links metabolism and gene regulation and plays a key role in multiple biological processes. We report that HBO1 functions as a lysine lactyltransferase to regulate transcription. Quantitative proteomic analysis further revealsed 95 endogenous Kla sites targeted by HBO1, with the majority located on histones.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Cervix Squamous Epithelium

DISEASE(S): Cervix Carcinoma

SUBMITTER: siyu wang

LAB HEAD: Kai Zhang

PROVIDER: PXD051415 | Pride | 2024-04-13

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	HeLa-Histone-La.raw	Raw
	HeLa-Histone-LactylationSites.txt	Txt
	HeLa-Kla-1.raw	Raw
	HeLa-Kla-2.raw	Raw
	HeLa-Kla-3.raw	Raw

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

Project description: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.

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Project description:Lysine lactylation (Kla) links metabolism and gene regulation and plays a key role in multiple biological processes. However, the regulatory mechanism and functional consequence of Kla remain to be explored. Here, we report that HBO1 functions as a lysine lactyltransferase to regulate transcription. Interestingly, CUT&Tag assays demonstrate that HBO1 is required for histone H3K9la on TSSs and the regulated Kla can facilitate in signaling pathways and progress of tumorigenesis. Our study reveals HBO1 serves as a lactyltransferase to mediate a histone Kla-dependent gene transcription.

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