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Cell debris was removed by centrifugation at 10 000 x g for 15 min. Trypsin digestion was performed by the FASP method. In brief, the clarified supernatant was added to a Microcon-30kDa centrifugal filter Unit (Merck Millipore, Burlington, USA) and centrifuged at 14 000 x g for 20 minutes. The filter units were washed with 8 M urea in 0.1 M HEPES (pH 7.8) and proteins were reduced with 10 mM DTT for 10 min at 37°C. After centrifugation proteins were alkylated with 0.05 M IAA for 5 min in darkness, again followed by centrifugation. Filter units were washed with 8 M urea in 0.1 M HEPES (pH 7.8) and subsequently with 0.1 M HEPES (pH 7.8). Digest was performed with 0.5 µg Trypsin (Pierce Thermo Fischer Scientific) at 37°C overnight. To elute the digested peptides, filter units were centrifuged, 50 µl of 0.5 M NaCl were added and again centrifuged. 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 Chloroplast Proteomics Probing 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 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