{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10460738_LFQ.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_LFQ_samples5-8.msf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_LFQ_samples1-4.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_AGO4_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_IgG_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10460738_AGO4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_AGO4_7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_MYC_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_WT_6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10460738_MYC.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_WT_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10460738_WT.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_IgG_8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_MYC_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10460738_IgG.raw"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_LFQ_samples1-4.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10461230_LFQ_samples5-8.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD059391/MercedesCarro10460738_LFQ.mgf"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["qf44@cornell.edu"],"submitter":["Qin Fu"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"software":["Not available"],"submitter_keywords":["Sex body","Spermiogenesis","Brg1","Aargonaute","Meiotic sex chromosome inactivation","Meiosis","Non-coding rna"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD059391"],"tissue":["Cell Culture"],"sample_protocol":["To gain insights into the mechanisms by which AGO proteins regulate gene expression during meiosis, we identified AGO3 and AGO4 interacting proteins by immunoprecipitation followed by Mass Spectrometry. AGO3 was immunoprecipitated from germ cell lysates of Ago3myc-flag mice using anti-MYC conjugated magnetic beads; as a negative control, we repeated this analysis using instead a wild-type lysate. Similarly, to identify AGO4 interacting proteins, we utilized an antibody against endogenous AGO4, employing anti-IgG antibodies to generate a background profile. We performed three biological replicates for each of the four conditions and calculated an abundance ratio between each AGO IP and respective control.We selected candidate interactors with consistent enrichment in at least two replicates. Samples were digested with Strap protocol by trypstion after reduction with DTT and alkylation with IDA.The tryptic digests were reconstituted in 2% acetonitrile (ACN) containing 0.5% formic acid (FA)for nanoLC-ESI-MS/MS analysis. The analysis was carried out using an Orbitrap FusionTM TribridTM (Thermo-Fisher Scientific, San Jose, CA) mass spectrometer equipped with a nanospray Flex Ion Source, and coupled with a Dionex UltiMate 3000 RSLCnano system (Thermo, Sunnyvale, CA).  The peptide samples (~0.6 μg for each sample) were injected onto a PepMap C-18 RP viper trapping column (5 µm, 100 µm i.d x 20 mm) at 20 µL/min flow rate for rapid sample loading and then separated on a PepMap C-18 RP nano column (2 µm, 75 µm x 25 cm) at 35 °C. The tryptic peptides were eluted in a 90 min gradient of 5% to 35% ACN in 0.1% formic acid at 300 nL/min, followed by an 8-min ramping to 90% ACN-0.1% FA and a 7-min hold at 90% ACN-0.1% FA. The column was re-equilibrated with 0.1% FA for 25 min prior to the next run.  The Orbitrap Fusion was operated in positive ion mode with spray voltage set at 1.9 kV and source temperature at 275°C. External calibration for FT, IT and quadrupole mass analyzers was performed. In data-dependent acquisition (DDA) analysis, the instrument was operated using FT mass analyzer in MS scan to select precursor ions followed by 3 second “Top Speed” data-dependent CID ion trap MS/MS scans at 1.6 m/z quadrupole isolation for precursor peptides with multiple charged ions above a threshold ion count of 10,000 and normalized collision energy of 30%.  MS survey scans at a resolving power of 120,000 (fwhm at m/z 200), for the mass range of m/z 375-1600.  Dynamic exclusion parameters were set at 50 s of exclusion duration with ±10 ppm exclusion mass width. All data were acquired under Xcalibur 4.4 operation software (Thermo-Fisher Scientific)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The samples were analyzed by nanoLC-MS/MS using CID acquire the raw files.  The mass spectra were searched against the Mus musculus Uniprot database with added your target protein's sequence with tag (Q00001) which contains 17068 sequences. Oxidation on M, deamination on N/Q; acetylation, M-loss and M-loss+acetylation on protein N-terminal were specified as dynamic modifications.Only high confidence peptides defined by Sequest HT with a 1% FDR by Percolator were considered for the peptide identification. The final protein IDs contained protein groups that were filtered with at least 2 peptides per protein. Relative quantitation of identified proteins between the two groups was determined by the Label Free Quantitation (LFQ) workflow in PD 2.4. After retention time alignment for each of the identified peptides across samples, the precursor abundance intensity for each peptide identified by MS/MS in each sample were automatically determined and their unique and razor peptides for each protein in each sample were summed and used for calculating the protein abundance by PD 2.4 software.  "],"omics_type":["Proteomics"],"labhead":["Qin Fu"],"instrument_platform":[""],"labhead_affiliation":["Cornell University"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["qf44@cornell.edu"],"publication":["Not available"],"submitter_affiliation":["Cornell University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Argonaute proteins regulate the timing of the spermatogenic transcriptional program","description":"Argonaute proteins are best known for their role in microRNA-mediated post-transcriptional gene silencing. Here, we show that AGO3, but not AGO2, localizes to the sex chromatin of pachytene spermatocytes nuclei, where together with AGO4, it is required for full transcriptional silencing of XY-linked genes. Using a triple Ago413-/- mouse, we show that AGO3 and AGO4 are key regulators of spermatogenesis, orchestrating program-wide expression of meiosis-related genes during prophase I, while maintaining silencing of spermiogenesis genes. Premature overexpression of spermiogenesis genes during prophase I in Ago413-/- mice results in subfertility, associated with severe spermiogenesis defects leading to altered sperm morphology and reduced fertilization capability. We also identify BRG1, a BAF complex subunit, as an AGO3 interactor. Loss of AGO3 and AGO4 results in increased BRG1 in spermatocytes, suggesting that AGO3 is needed to help remove BRG1 from the XY chromatin during meiotic sex chromosome inactivation and indicating a role for AGO3 in transcriptional control during meiosis through interaction with the chromatin remodeling 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