{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074595/Liver_report.pg_matrix.tsv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074595/Heart_report.pg_matrix.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074595/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074595/20251216_AV_David_H01_2025-12-17_12310.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["akos.vegvari@ki.se"],"submitter":["Akos Vegvari"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Mitochondria","Mtdna","Mouse models","Polrmt"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074595"],"tissue":["Heart","Liver"],"sample_protocol":["Mouse heart and liver tissues were thawed on ice and cut into small pieces before transferring them to a prefilled tube containing 400 µm LoBind silica beads and supplemented with 300 µL of 8M urea in 100 mM ammonium bicarbonate (Ambic) and 100x Halt protease inhibitor. The samples were sonicated in water bath for 5 min and frozen for a short time before homogenized using Disruptor Genie at maximal speed on 2700 rpm for 2 min, incubated on ice for 2 min, repeating these steps three times. The samples were then centrifuged at 10,000g for 10 min at 4°C. The supernatant was collected and 200 µL of 50 mM Ambic was added before protein concentration was determined by Qubit broad range assay (Thermo). An aliquot of 5 µg samples was reduced with 2.5 µL of 100 mM dithiothreitol at 37°C for 45 min, alkylated with 7.5 µL of 100 mM iodoacetamine at room temperature for 30 min in dark and finally digested with addition of 0.1 µg of sequencing grade modified trypsin (Promega) and incubated for 16 h at 37°C.  The digestion was stopped with 3 µL formic acid. The samples were cleaned on a C18 StageTip (Thermo Fisher Scientific), dried using a vacuum concentrator (Eppendorf).  Peptides were reconstituted in solvent A and 200 ng samples loaded on Evotip Pure (Evosep Biosystems) tips following the manufacturer's sample loading protocol. Peptide separation was performed on an Evosep Eno system (Evosep Biosystems) using the standardized 30 samples per day (SPD) method, which provides a 44-minute gradient optimized for comprehensive proteome coverage. Peptides were separated on a PepSep column (15 cm length × 150 μm inner diameter) packed with 1.9 μm C18 particles (Bruker). The column was operated at room temperature without additional heating. The 30 SPD method uses a pre-formed gradient approach where peptides are eluted from the Evotip with increasing concentrations of acetonitrile, then diluted and transferred to a storage loop before final separation on the analytical column. This design maximizes chromatographic peak capacity while minimizing overhead time between injections, achieving high MS utilization (>90%). The Evosep Eno system was coupled online to a timsTOF HT mass spectrometer (Bruker Daltonics) equipped with a fourth-generation TIMS-XR analyzer cartridge. Data acquisition was performed in data-independent acquisition parallel accumulation-serial fragmentation (dia-PASEF) mode, which combines trapped ion mobility spectrometry (TIMS) with data-independent acquisition. The MS1 survey spectra covered a mass range of 100-1700 m/z. For MS2 fragmentation, twelve isocentric isolation windows were defined spanning 390-1250 m/z in the mass dimension and 0.84-1.31 1/K0 in the ion mobility dimension. The dia-PASEF acquisition scheme was optimized to balance precursor coverage, selectivity, and sensitivity for the 44-minute gradient, with sufficient data points acquired across each chromatographic peak for accurate quantification. The TIMS-XR analyzer provided enhanced ion capacity (5-fold increase over previous generation) and improved dynamic range through its doubled ion storage volume, quadrupolar exit design, and optimized gas velocity profile. These features enabled better handling of complex samples and higher peptide loading masses without ion suppression or detector saturation."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Raw data files (.d format) were processed using DIA-NN software (version 2.2.0) for peptide and protein identification and quantification. Searches were performed against a theoretically generated spectral library using the following parameters: trypsin/P as the protease with a maximum of one missed cleavage allowed; carbamidomethylation of cysteine residues as a fixed modification; oxidation of methionine and N-terminal acetylation as variable modifications. A false discovery rate (FDR) threshold of 1% was applied at the peptide precursor level. MS1 and MS2 mass tolerances were automatically determined by DIA-NN's optimization algorithms. The software utilized neural networks and interference correction to enable deep proteome coverage while maintaining high confidence identifications. All other search parameters were maintained at DIA-NN default settings."],"omics_type":["Proteomics"],"labhead":["Akos Vegvari"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Karolinska Institutet, Stockholm, Sweden"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["akos.vegvari@ki.se"],"submitter_affiliation":["Karolinska Institutet"],"submitter_country":["Sweden"],"additional_accession":[]},"is_claimable":false,"name":"Pathogenic POLRMT variants in mice impair mtDNA transcription and affect perinatal survival","description":"Mitochondrial gene expression is essential for oxidative phosphorylation (OXPHOS) that generates the bulk of the cellular ATP, and dysfunctional mitochondria is a common cause of human metabolic diseases. Recently, the first pathogenic variants in the only known mitochondrial RNA polymerase (POLRMT) were described. Patients present with a wide variety of clinical manifestations, such as hypotonia, short stature and developmental delay. Here, we modeled two human pathogenic POLRMT variants by creating the corresponding substitutions in mice: the dominant S582F and the recessive R984C variant. Mice homozygous for the R984C variant showed perinatal lethality without apparent embryonic developmental defects, thus showing that POLRMT has a critical role in the transition to oxidative metabolism at birth. Mice carrying the S582F variant were viable and exhibited decreased mitochondrial transcript levels due to impaired de novo transcription. However, mtDNA levels and in organello mtDNA replication remained normal, which recapitulates the molecular phenotypes observed in the patients. Altogether, our findings indicate that the conserved arginine near the active site is essential for POLRMT function, while the serine in the intercalating hairpin of the N-terminal domain is required for transcription but not primase activity. This study highlights genotype–phenotype differences and provides new insights into POLRMT 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