{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_UT-R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/Asc_008737_UT-R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/Asc_008739_IAA-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_IAA-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/Asc_008745_IAA-R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_IAA-R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/Asc_008727_IAA-R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_UT-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_UT-R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/Asc_008743_UT-R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/Asc_008723_UT-R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_IAA-R1.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/Acetylome.mzid"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_UT-R2.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_IAA-R3.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_IAA-R2.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_UT-R1.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_IAA-R1.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/AcK_UT-R3.mgf"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD079432/TotalProteome.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["yohann.coute@cea.fr"],"submitter":["Yohann Couté"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Toxoplasma","Tggcn5b","Nanolc-ms/ms","Acetylation"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079432"],"sample_protocol":["Human primary fibroblasts (HFFs, ATCC® CCL-171™) were cultured in Dulbecco's Modified Eagle Medium (DMEM) (Invitrogen) supplemented with 10% heat-inactivated fetal bovine serum (FBS) (Invitrogen), 10 mM (4-(2-hydroxyethyl)-1-piperazine-ethanesulfonic acid) (HEPES) buffer pH 7.2, 2 mM L-glutamine and 50 μg/ml penicillin and streptomycin (Invitrogen). Cells were incubated at 37°C and 5% CO2. Degradation of POI (protein of interest)-mAID-HA was achieved with 3-indoleacetic acid (IAA, Sigma-Aldrich # 45533). A stock of 500 mM IAA dissolved in 100% EtOH at a ratio of 1:1,000 was used to degrade mAID-tagged proteins to a final concentration of 500 μM. The mock treatment consisted of an equivalent volume of 100% EtOH at a final concentration of 0.0789% (wt/vol). To monitor the degradation of mAID-tagged POI, parasites grown in HFF monolayers were treated with auxin or ethanol alone for various time intervals at 37 ̊C. After treatment, parasites were harvested. For each replicate (n=3 per condition), 2 mg of proteins in 8M urea-containing buffer were incubated for 1h at 37°C with 20mM of dithiothreitol before alkylation with 55mM of iodoacetamide for 45 min at room temperature in the dark. The samples were then diluted using ammonium bicarbonate to obtain a urea concentration of 4M. Proteins were digested with modified trypsin (sequencing grade, Promega) at a ratio of 1:100 during 4 h at 37 °C. The samples were diluted again using ammonium bicarbonate to obtain a urea concentration of 1 M. Proteins were then digested again with modified trypsin at a ratio of 1:100 overnight at 37 °C. the resulting peptides were purified by reverse phase chromatography (Oasis HLB, Waters) before drying down.  One µg of peptides was used for MS-based quantitative analysis of total proteomes and 1 mg for enrichment of acetylated peptides using the PTMScan HS Acetyl-Lysine Motif [Ac-K] Kit (Cell Signaling Technology). Peptides obtained after immunoenrichment were desalted (BioSPE PurePep, Affinisep). The samples were analysed by online nanoliquid chromatography coupled to mass spectrometry (Ultimate 3000 RSLCnano and Orbitrap Exploris 480, Thermo Fisher Scientific, for total proteome and Vanquish Neo, Thermo Fisher Scientific and Orbitrap Ascend Tribrid, Thermo Fisher Scientific, for acetylome) operating in data-independent acquisition mode (total proteome) or data-independent acquisition mode (acetylome). Peptides were sampled on a 300 μm x 5 mm PepMap C18 precolumn (Thermo Fisher Scientific) and separated in a 75 μm x 250 mm C18 column (Aurora Ultimate, 1.7 μm, IonOpticks) using a 2h-long acetonitrile gradient."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For total proteome analysis, peptides and proteins were identified and quantified by DIA-NN (version 1.9.2) using a library-free mode with the Toxoplasma gondii database (ME49 taxonomy, version 68 downloaded from ToxoDB), the Uniprot database (Homo sapiens taxonomy, 202504 version) and a homemade database containing the sequences of contaminants classically identified in proteomic datasets. The digestion enzyme was set to Trypsin/P, up to 2 missed cleavages were allowed and peptide range was set from 6 to 30 amino acids. Precursor charge range was set from 1 to 4 while precursor m/z range was set to 400-1001 m/z and fragment ion m/z range to 120-2000 m/z. Carbamidomethylation (C) was used as fixed modification and N-term M excision, Oxidation (M) and Acetylation (N-Ter) were used as variable modifications. Precursor FDR was set to 1% and the match between runs (MBR) option was activated. For acetylome analysis, peptides and proteins were identified with Mascot (version 3.1.0, Matrix Science), through concomitant searches against the Toxoplasma gondii database (ME49 taxonomy, downloaded from ToxoDB), the Uniprot database (Homo sapiens taxonomy), and a homemade database containing the sequences of classical contaminant proteins found in proteomic analyses (human keratins, trypsin...). Trypsin/P was chosen as the enzyme and four missed cleavages were allowed. Precursor and fragment mass error tolerances were set at respectively at 10 and 20 ppm. Peptide modifications allowed during the search were: Carbamidomethyl (C, fixed), Acetyl (Protein N-term, variable), Oxidation (M, variable) and Acetyl (K, variable). The Proline software (version 2.3.3) was used for the compilation, grouping, and filtering of the results (conservation of rank 1 peptides, peptide length ≥ 6 amino acids, false discovery rate of peptide-spectrum-match identifications < 1%, and minimum of one specific peptide per identified protein group)."],"omics_type":["Proteomics"],"labhead":["Yohann Couté"],"instrument_platform":[""],"labhead_affiliation":["EDyP"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)","Toxoplasma Gondii"],"submitter_mail":["yohann.coute@cea.fr"],"publication":["Not available"],"submitter_affiliation":["EDyP"],"submitter_country":["France"],"doi":["10.6019/PXD079432"],"additional_accession":[]},"is_claimable":false,"name":"MS-based proteomic analysis of TgGCN5b-dependent acetylome and proteome","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 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