{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057465/mqpar.xml"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057465/Col-0_B2_3_GB5_1_4091.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057465/gatB-1_B2_3_GB6_1_4093.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057465/Col-0_B2_1_GB1_1_4083.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057465/MQ_combined.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057465/Col-0_B2_1_GB1_1_4080.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057465/gatB-1_B2_2_GB4_1_4089.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057465/Col-0_B2_4_GB7_1_4095.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057465/gatB-1_B2_1_GB2_1_4085.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057465/gatB-1_B2_4_GB8_1_4097.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057465/Col-0_B2_2_GB3_1_4087.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["kunz@lmu.de"],"submitter":["Benjamin Brandt"],"technology_type":["Mass Spectrometry","Gel-based experiment"],"software":[""],"submitter_keywords":["Mistranslation","Dda","Gatcab"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057465"],"tissue":["Rosette"],"sample_protocol":["21-24 days old plants used for the chloroplast enrichment were grown at the same time at standard growth conditions defined in the “experimental model and study participant details” section. To reduce starch accumulation in the chloroplasts, plants were kept dark for 16h before chloroplast enrichment. Chloroplasts were enriched by disrupting ~3g leafs in cold CP-MT extraction buffer (0.3 M Sorbitol, 5mM MgCl2, 5 mM EDTA, 20 mM HEPES-KOH pH 8.0 and 10 mM NaH2CO3) using a polytron mixer. The resulting suspension was filtered through two layers of Miracloth. Chloroplasts were then pelleted by centrifugation at 1500 g and 4°C for 5 min. The chloroplast containing pellet was then washed with chloroplast extraction buffer, pelleted again and then used in subsequent analyses. Enriched chloroplasts (see above) were used immediately after extraction. Here, the chlorophyll concentration of all samples was assessed in 80% acetone using a photometer. Subsequently, the volume corresponding to 30 µg chlorophyll was used for all samples for the BN-PAGE used for mass spectroscopy. gatb-1 only has 73% of the Chl A + B content (in μmol/g FW) of WT plants (see Figure 1I). Thus, to normalize the loading for the analytical BN-PAGE to the fresh weight, the volumes for 30 µg for WT and 21.9 µg gatb-1 were used. Chloroplasts for both approaches were then pelleted at 500g and 4°C for 3 min, resuspended in ACA buffer (50 mM Bis-Tris pH 7.5, 750 mM Aminocaproic acid and 0.5 mM EDTA-Na2), supplemented with dodecyl maltoside to a final concentration of 0.5% (w/v), incubated on ice for 25 min and finally centrifuged at 16000g and 4°C. BN-loading dye (final concentrations: 68 mM Aminocaproic acid and 0.45% (w/v) Coomassie brilliant blue G-250) was added to the supernatant before loading half of the samples on 4-12% Acrylamide gels (final concentration of gel buffer: 500 mM Aminocaproic acid and 50 mM Bis-Tris pH 7.0). The gel was run using blue cathode buffer (50 mM Tricine, 15 mM Bis-Tris and 0.2% Coomassie brilliant blue G-250) and anode buffer (50 mM Bis-Tris pH 7.0) until the sample dye front reached 2/3rd of the gel. Then the cathode buffer was changes to clear cathode buffer without Coomassie brilliant blue. When the dye front reached the bottom of the gel, the gel was removed from the glass plate and imaged. A high molecular weight band (PSI, PSII-d and ATP-synth.) was excised. Excised Coomassie-stained gel pieces from BN-PAGE gels were washed three times with water and cut into small pieces. Gel pieces were washed twice for 10 min each with 20 mM ammonium bicarbonate (ABC) and acetonitrile (ACN). Subsequently, proteins were reduced with 10 mM DTT at 56°C for 30 min. Samples were washed with ACN for 10 min followed by alkylation with of 55 mM IAA for 30 min in darkness. The samples were washed twice for 10 min each with ABC and ACN, and then digested overnight with 0.3 μg Trypsin (Pierce Thermo Fischer Scientific) at 37°C. Digested peptides were extracted with 5% formic acid (FA), 50% ACN, 50% ACN and 1% FA, each for 15 min at 37°C. All extractions were pooled and peptides were dried in a vacuum centrifuge.  Digested peptides from all above protocols were purified using home-made C18 stage tips. The tips were activated with 100% methanol and equilibrated with 0.5% FA before loading the peptides. After loading, the tips were washed with 0.5% FA. Peptides were eluted with 80% ACN with 0.1%FA.  For LC-MS/MS analysis 1 µg of peptides were separated over linear gradients from 5% to 80% (v/v) ACN at a constant flow rate of 250 nl/min on a nano-LC system (Ultimate 3000 RSLC, Thermo Fisher Scientific, Waltham, MA, USA). Gradient lengths varied according to sample complexity: total protein sample 90 min, chloroplast sample 60 min, gel sample 30 min. The LC was equipped with an Acclaim Pepmap nano-trap column (C18, 100 Å, 100 μm × 2 cm) and an Acclaim Pepmap RSLC analytical column (C18, 100 Å, 75 μm × 50 cm), both from ThermoFisher Scientific. The column temperature was maintained at 50°C throughout the run. MS/MS was performed on an Impact II high-resolution Q-TOF (Bruker Daltonics, Bremen, Germany) using a CaptiveSpray nano electrospray ionization (ESI) source (Bruker Daltonics). MS1 spectra with a mass range from m/z 200–2000 were acquired at 3 Hz, and the 18 most intense peaks were selected for MS/MS analysis with an intensity-dependent spectrum acquisition rate of 4 to 16 Hz. The dynamic exclusion duration was set to 0.5 minutes."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw data files were analyzed using MaxQuant software (v2.1.4.), with peak lists compared against the Arabidopsis reference proteome from UniProt (www.uniprot.org). LFQ quantification including 'match-between-runs' was enabled. Oxidation (M), Acetyl (Protein N-term), Asn -> Asp, and Gln -> Glu were included as variable modifications, while Carbamidomethyl (C) was set as a fixed modification. IBAQ protein quantification was enabled. All other settings were kept at default values."],"omics_type":["Proteomics"],"labhead":["Hans-Henning Kunz"],"instrument_platform":[""],"labhead_affiliation":["LMU Munich Plant Biochemistry and Physiology, Germany"],"submission_type":["PARTIAL"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"submitter_mail":["brandt@lmu.de"],"publication":["10.1073/PNAS.2537357123"],"submitter_affiliation":["LMU Munich\nPlant Biochemistry and Physiology"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Arabidopsis BN-PAGE Proteomics Probing GatCAB-dependent Mistranslation","description":"Protein translation is a fundamental principle in cell biology. It requires transfer RNAs (tRNAs) loaded with their cognate amino acid to ensure the accurate incorporation of amino acid into the nascent peptide chain. Bacteria, mitochondria, and plastids synthesize glutaminyl -tRNAs (Gln-tRNAGln) for protein synthesis via an indirect pathway. tRNAGln is initially charged with glutamate by a non-discriminating aminoacyl-tRNA synthetase. Subsequently, tRNA-attached glutamine is produced by transamidation of the Glu-tRNAGln via the aminoacyl-tRNA amido-transferase complex GatCAB. Impaired function of amido-transferases has mostly negative effects in humans, yeast and bacteria. Interestingly however, in bacteria protein mistranslation through changed amido-transferase activity was shown as specialized strategy to survive adverse conditions, such as reactive oxygen stress, UV-light or inhibitor treatments. The consequences of decreased amido-transferase activity in plant and especially its plastids are unknown. Tampering with the plant amido-transferase should result in amino acid misincorporation for proteins synthesized in plastids and mitochondria while nuclear encoded proteins should not exhibit increased rate of Gln to Glu substitutions. Using this dataset, we aim to investigate this hypothesis assembled photosynthetic complexes in a band cut from a BN-PAGE of chloroplasts of wt and gatb-1 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