{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057466/mqpar.xml"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057466/gatB_2_GC4_1_4597.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057466/WT_3_GC5_1_4599.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057466/gatB_3_GC6_1_4601.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057466/WT_4_GC7_1_4603.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057466/MQ_combined.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057466/gatB_4_GC8_1_4605.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057466/WT_1_GC1_1_4591.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057466/WT_2_GC3_1_4595.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057466/gatB_1_GC2_1_4593.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","Gatcab"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057466"],"tissue":["Leaf","Rosette"],"sample_protocol":["Total proteins were extracted from 500 ul of frozen ground powder of 4 biological replicates of either plYFP-WT or plYFP-gatb-1 leaf material with 2 ml of extraction buffer (50 mM Tris pH 7.5, 150 mM NaCl, 2.5 mM EDTA, 10% Glycerol, 0.5% NP-40, 5 mM DTT, 1x plant protease inhibitor cocktail) and solubilized for 20 min on ice.Cell debris was removed by centrifugation at 25,000 g and 4°C for 10 min. To supernatant homemade GFP-trap based on a double ankyrin-repeat protein was added and the mixture was incubated on a rotation shaker for 2h at 4°C. The resin was pelted by centrifugation at 500g for 1 min and washed 4 times with wash buffer (50 mM Tris pH 7.5, 150 mM NaCl, 2.5 mM EDTA, 10% Glycerol, 0.5% NP-40). After pelleting the resin after the last wash step, the resin was resuspended in 1.5 x SDS-Loading dye, cooked at 80°C, soun at 500g for 1min and the supernatant was subjected to SDS-PAGE in a 4-20% Gel (Mini-PROTEAN TGX; Biorad). Gels were stained with coomassier brilliant blue and bands corresponding to YFP were cut out. Excised Coomassie-stained gel pieces from SDS-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 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"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Immunoprecipitated plYFP data was analyzed using MaxQuant software (v2.2.0) matching peak to the Arabidopsis reference proteome from UniProt (www.uniprot.org) to which the sequence of the plastid expressed YFP was added. Additionally, GFP and YFP was removed from the common lab contaminants list for the search. 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)"],"publication":["10.1073/PNAS.2537357123"],"submitter_mail":["brandt@lmu.de"],"submitter_affiliation":["LMU Munich\nPlant Biochemistry and Physiology"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Arabidopsis Immunoprecipitated Plastid Expressed YFP 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 on plastid expressed YFP which was immunoprecipitated from WT or gatb-1 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