Mass spectrometry-based proteomic characterization of TgGCN5b, TgPHD1, TgPZP1, TgGNAT1 and TgGNAT2 interactomes
Ontology highlight
ABSTRACT:
INSTRUMENT(S):
ORGANISM(S): Homo Sapiens (human) Toxoplasma Gondii Rh
SUBMITTER: 
Yohann Couté
LAB HEAD: Yohann Couté
PROVIDER: PXD072342 | Pride | 2026-07-25
REPOSITORIES: Pride
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| GCN5b-PHD1-mock.mzid | Mzid | |||
| GCN5b-R1.raw | Raw | |||
| GCN5b-R1_40.mgf | Mgf | |||
| GCN5b-R1_55.mgf | Mgf | |||
| GCN5b-R2.raw | Raw |
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Project description: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 evaluated the impact of TgGCN5b depletion on lysine acetylome and total proteome of infecting parasites.
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