The compound identities were verified by mass and retention time matches to authenticated standards (Sigma-Aldrich, P8001-5G).
"],"repository":["MetaboLights"],"study_status":["Public"],"ptm_modification":[""],"instrument_platform":["Liquid Chromatography MS - negative - reverse-phase"],"chromatography_protocol":["The PPY was analyzed by a QTRAP mass spectrometer (6500, AB Sciex) equipped with UHPLC (1290, Agilent) and a HYPERCARB column (150 mm × 2.1 mm, 5 μm, Thermo). The injection volume was 10 μL. The mobile phase A was 0.1% ammonium hydroxide, 10 mM ammonium formate in water, and B was acetonitrile. The column was maintained at 40 °C with a flow rate of 0.3 mL min-1, and the gradient of B was as follows: 0 min, 5%; 1 min, 5%; 6 min, 95%; 8 min, 95%; 8.1 min, 5%; 12 min, 5%.
"],"publication":["A Plastoglobuli-Localized Enzyme Links Phenylalanine Biosynthesis to Translational Homeostasis in Maize."],"submitter_affiliation":["CAS Center for Excellence in Molecular Plant Sciences"],"submitter_name":["Xing Huang"],"organism_part":["endosperm","leaf"],"technology_type":["mass spectrometry assay"],"disease":[""],"extraction_protocol":["For PPY extraction, the same amount of tissue was homogenized in 0.5 mL of 1 mM carbonate-bicarbonate buffer (pH 9.6) under identical conditions. After centrifugation (15,000 g, 20 min, 4 °C), transfer 300 µL of supernatant to a new tube. Add 500 µL of methanol: acetonitrile (1:1, v/v), vortex for 3 min, and incubate at –20 °C for 2 h to precipitate proteins. After centrifugation (15,000 g, 20 min, 4 °C), collect 200 µL of supernatant into an insert-equipped vial for analysis.
"],"organism":["Zea mays"],"full_dataset_link":["https://www.ebi.ac.uk/metabolights/MTBLS14853"],"author":["Xing Huang. CAS Center for Excellence in Molecular Plant Sciences. huangxing@cemps.ac.cn.","Yongrui Wu. CAS Center for Excellence in Molecular Plant Sciences. yrwu@cemps.ac.cn."],"data_transformation_protocol":["Instrument control and data acquisition were performed using Analyst 1.6.3 software (AB SCIEX), and data processing was performed using MultiQuant 3.0.2 software (AB SCIEX).
"],"study_factor":["Plant part"],"submitter_email":["huangxing@cemps.ac.cn"],"sample_collection_protocol":["The different genotype plant stem were collected in the heading stage and immediately frozen in liquid nitrogen. The stem was then ground into fine powder. The 18-DAP B104 and adt2.2 endosperm were collected and immediately frozen in liquid nitrogen. The endosperm was then ground into fine powder.
"],"omics_type":["Metabolomics"],"study_design":["Metabolomics","Zea mays","targeted analysis","ADT2.2","liquid chromatography-tandem mass spectrometry","Maize","experimental blank","AB SCIEX QTRAP 6500","Agilent 1290 Infinity HPLC","endosperm","leaf"],"curator_keywords":["Metabolomics","Zea mays","targeted analysis","ADT2.2","liquid chromatography-tandem mass spectrometry","Maize","experimental blank","AB SCIEX QTRAP 6500","Agilent 1290 Infinity HPLC","endosperm","leaf"],"mass_spectrometry_protocol":["All analytes were detected using Multiple Reaction Monitoring (MRM) mode. The optimized ESI operating parameters for negative mode were: ion spray voltage, -4.5 kV; ion spray temperature, 500 °C; curtain gas, 35 psi; ion source gas 1, 50 psi; ion source gas 2, 50 psi.
"],"additional_accession":[]},"is_claimable":false,"name":"A Plastoglobuli-Localized Enzyme Links Phenylalanine Biosynthesis to Translational Homeostasis in Maize","description":"Aromatic amino acids are essential precursors for numerous plant metabolites, with phenylalanine (Phe) forming the basis of the phenylpropanoid pathway. Here, we reveal a critical mechanism for Phe biosynthesis in maize, demonstrating that all seven arogenate dehydratases (ADTs) are specifically localized to plastoglobuli (PGs) in chloroplasts, and ADT2.2 shows high catalytic activity towards arogenate and prephenate. This discovery establishes PGs as a site for Phe synthesis. Genetic analysis confirms that only ADT2.2 is indispensable for plant and seed development, with its loss causing a severe Phe deficiency in seeds. This metabolic blockage directly reduced the tRNAPhe-GAA charging, thereby repressing protein translation. Crucially, we uncover that Phe starvation disproportionately affects the decoding efficiency of wobble-paired codons, increasing ribosome pausing. Our work provides biochemical and genetic evidence that PGs-localized ADT2.2 catalyzes Phe synthesis and reveals a link between amino acid availability and codon-specific translation dynamics.","dates":{"publication":"2026-06-25","submission":"2026-06-24"},"accession":"MTBLS14853","cross_references":{}}