{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057463/mqpar.xml"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057463/WT_1_GB1_1_5018.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057463/WT_3_GB5_1_5026.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057463/WT_4_GB7_1_5030.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057463/gatB_2_GB4_1_5024.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057463/gatB_3_GB6_1_5028.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057463/gatB_1_GB2_1_5020.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057463/MQ_combined.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057463/gatB_4_GB8_1_5032.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057463/WT_2_GB3_1_5022.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":["Mistranslation","Dda","Rubisco","Gatcab"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057463"],"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. To lyse enriched chloroplasts the chloroplasts were resuspended in chloroplast burst buffer (10 mM Hepes pH 7.5, 10 mM MgCl2) and passed through a syringe needle 15-20 times. Subsequently, NaCl was added to gain a final concentration of 150 mM. To remove thylakoind membranes the suspension was centrifuged at 5,000 g and 4°C for 5 min. Supernatant was transferred to a fresh tube and residual liquid was carefully removed. The thylakoid containing pellet was resuspended in 8 M Urea and flash frozen in liquid nitrogen (thylakoid fraction). To further remove residual thylakoid, inner and outer envelope membranes as well as aggregates, the supernatant was subsequently centrifuged twice at 45,000 g and 4°C for 15 min. The supernatant was immediately subjected to size exclusion chromatography (SEC). Here, a Superdex 200 Increase 10/300 GL column was equilibrated with SEC buffer (10 mM Hepes pH 7.5, 150 mM NaCl, 4% Glycerol) and then 300 µl of isolated stroma were injected and eluted. 500 µl fractions were collected. Fractions 9-12 of each run were combined and concentrated to 70-100 µl using a centrifugal concentrator (MWCO 100 kDa; Vivaspin). Concentrated SEC fractions (equivalent to 50 µg protein) were resuspended in 250 µl extraction buffer, sonicated, incubated at 60°C and centrifuged as described above for plant powder. 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":[""],"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 L8S8 RuBisCO 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 for fully assembled L8S8 RuBisCO isolated by size exclusion chromatography.","dates":{"publication":"2026-06-08","submission":"2024-11-03"},"accession":"PXD057463","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52639","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:441772","NEWT:48106","NEWT:202956","NEWT:295027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