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Mass spectrometry-based proteomic characterization of TgGCN5b and TgGNAT2 interactomes

ABSTRACT: Histone acetylation, a fundamental epigenetic mechanism that controls gene activity, is essential for the developmental plasticity and virulence of the parasite Toxoplasma gondii. However, how this parasite organizes and deploys its acetyltransferase machinery has remained unclear. We show that T. gondii rewired this process using a plant-like system built around the acetyltransferase TgGCN5b, which differs from the typical SAGA complex found in other eukaryotes. We complete our interactome analysis by characterizing TgGCN5b interactome in PHD1 KD or AP2XI-2 and AP2XII-1 KD parasites, TgGCN5b interactome from simple and double purifications, and TgGNAT2 interactome.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human) Toxoplasma Gondii

SUBMITTER: Yohann Couté

LAB HEAD: Yohann Couté

PROVIDER: PXD079431 | Pride | 2026-07-25

REPOSITORIES: Pride

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			Action	DRS
	FLAG-HA.raw	Raw
	FLAG-HA_CV-40.mgf	Mgf
	FLAG-HA_CV-55.mgf	Mgf
	FLAG-HA_Results.mzid	Mzid
	FLAG.raw	Raw

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