{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/mqpar_uniprot.xml"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/analysis.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/Col-0_4_GC4_1_4350.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatA_4_GC5_1_4353.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatA_2_GB5_1_4336.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatA_1_GB2_1_4327.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatB_1_GB3_1_4329.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/Col-0_3_GC1_1_4341.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatB_3_GC3_1_4347.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatB_2_GB6_1_4339.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/Col-0_2_GB4_1_4333.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/Col-0_1_GB1_1_4324.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatA_3_GC2_1_4345.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/Col-0_4_GC4_1_4351.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatB_4_GC6_1_4357.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatB_3_GC3_1_4348.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/Col-0_3_GC1_1_4342.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatB_1_GB4_1_4330.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatA_2_GB5_1_4335.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatA_4_GC5_1_4354.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/Col-0_2_GB4_1_4332.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatA_1_GB2_1_4326.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/Col-0_1_GB1_1_4323.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatB_2_GB6_1_4338.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatB_4_GC6_1_4356.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057453/gatA_3_GC2_1_4344.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["kunz@lmu.de"],"submitter":["Benjamin Brandt"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":["Dda","Mistranslation","Gatcab"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057453"],"tissue":["Rosette"],"sample_protocol":["145 T2 plants of amiGatA were grown alongside WT and gatb-1. After 28 days of growth, per biological WT and gatb-1 replicate 4 plants and per amiGatA biological replicate 35 rosettes were pooled and immediately flash frozen in liquid nitrogen. A total of 4 biological replicates per genotype was prepared. Frozen plant material was ground to fine powder using a precooled mortar and pestle. 100 mg of the powder was resuspended in 0.3 ml of extraction buffer (100 mM HEPES pH 7.5, 150 mM NaCl, 10 mM DTT, 6 M Guanidine Chloride, Roche cOmplete™ Protease Inhibitor Cocktail). Each sample underwent sonication using a Branson Sonifier B-12 (Branson Ultrasonics, Danbury, USA) for 3 cycles of 20 seconds and samples were subsequently incubated at 60°C for 10 min. Cell debris was removed by centrifugation at 10 000 x g for 15 min. Proteins were precipitated with the chloroform-methanol. For this, methanol/chloroform and water were added to the clarified sample in a 4:2:3 ratio. The mixture was centrifuged for 10 min at 10 000 x g, the precipitated protein accumulating at the interphase was retained and washed five times with methanol. The protein pellet was dried and solubilized in 3 M Urea/2 M Thiourea in 50 mM HEPES (pH 7.8). The total protein concentration was determined using the Pierce 660 nm Protein Assay Kit (Pierce, Thermo Fischer Scientific). 100 µg of protein was reduced with 10 mM DTT for 30 min at 37°C and alkylated with 50 mM iodoacetamide (IAA) for 20 min at RT in darkness, followed by overnight digestion with 1 µg Trypsin (Pierce Thermo Fischer Scientific), at 37°C.analysis. Digested peptides were purified using home-made C18 stage tips (Rappsilber et al., 2003). 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":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["LMU Munich Plant Biochemistry and Physiology, Germany"],"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 GatA Mutant 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 in in mutant Arabidopsis thaliana plants which express an amiRNA against GatA 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