Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/SN_250226_FDR1_Peptides_ControlsCombined.xlsxftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/SN1_14_HA_TOC75_3_ingelMS_FDR1__Final.xlsxftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/SN_APMS_TOC75_FDR1_251107_LFQ.xlsxftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/SN_250226_FDR1_Proteins_ControlsCombined.xlsxftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/checksum.txtftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX02_MF_211220_MF_SN2-test_122.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN3_test_026.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN10_test_035.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN1_test_022.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_VR_251125_SN_WT_2_110.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN6_test_030.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN12_test_041.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN14_test_045.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_VR_251125_SN_HA75_3_118.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_VR_251125_SN_WT_1_108.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_VR_251125_SN_HA75_1_114.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_VR_251125_SN_WT_3_112.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN4_test_024.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN5_test_028.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN9_test_037.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX02_MF_211220_MF_SN7-test_124.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN8_test_033.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN11_test_039.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_MF_220106_SN13_test_043.rawftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD072672/QEX03_VR_251125_SN_HA75_2_116.rawprimaryOK200marjorie.fournier@bioch.ox.ac.ukVaishnavi RavikumarAffinity purification coupled with mass spectrometry proteomicsMass SpectrometryGel-based experimenthttps://www.ebi.ac.uk/pride/archive/projects/PXD072672Post immunoprecipitation, the beads were washed gently 3x times in PBS. Beads were then equilibrated in buffer containing 8 M urea, 0.1 M ammonium bicarbonate for 10 min at RT and subsequently reduced with 10 mM tris(2-carboxyethyl)phosphine) and alkylated (in the dark with 50 mM 2-chloroacetamide, for 30 min each at room temperature, at 750 rpm. This was proceeded with a pre-digestion with endoprotease LysC (Wako; 1:100) at 37 °C for 2 h at 750 rpm, followed by 16-18 h digestion with trypsin (Promega, 1:40), supplemented with 2 mM calcium chloride at 37 °C at 750 rpm. The supernatant was collected post digestion and acidified with 5% formic acid. Digested peptides were loaded onto C18 stage tips (1), pre-activated and equilibrated with 100 % acetonitrile and 0.1 % trifluoracetic acid. Subsequently, peptides were washed with 0.1 % trifluoracetic acid and eluted in 50 % acetonitrile / 0.1 % trifluoracetic acid. Eluted peptides were dried in a speed-vac before injection. 3 biological replicates were performed.PrideNot availableTandem mass (MS/MS) spectra were searched using Sequest HT in Proteome discoverer software version 1.4 were searched against a protein sequence database containing 18,300 protein entries from the Arabidopsis thaliana database (Proteome ID UP000006548) and the tagged Toc75 protein sequence along with 292 common contaminants. During database searching cysteines (C) were considered to be fully carbamidomethylated (+57.0215, statically added), methionine (M) to be fully oxidised (+15.9949, dynamically added), all N-terminal residues to be acetylated (+42.0106, dynamically added), asparagine (N) and glutamine (Q) to be fully deamidated (+0.984, dynamically added). Two missed cleavages were permitted. Peptide mass tolerance was set at 20ppm on the precursor and 0.6 Da on the fragment ions. Data was filtered at FDR below 1% at PSM level.ProteomicsDr MarjoriePARTIALDepartment of Biochemistry, University of Oxford, United KingdomArabidopsis Thaliana (mouse-ear Cress)Not availablevaishnavi.ravikumar@gmail.comDept. of Biochemistry, University of OxfordUnited KingdomfalseAssembly of two functionally-distinct protein import complexes in the outer membrane of plant chloroplasts (interactome data)The TOC protein translocon delivers thousands of nucleus-encoded proteins to chloroplasts and to related non-photosynthetic plastids. It comprises the β-barrel channel, Toc75, and multiple isoforms of receptor GTPases, Toc33 and Toc159. However, exactly how TOC complexes are assembled in different plastid types, is not known. Here, we present detailed characterization of two distinct TOC complexes, TOC-P and TOC-N, from photosynthetic chloroplasts and non-photosynthetic plastids, respectively. The assembled complexes are distinguished by having different sets of receptors, but both possess Toc75 which we identify as a central hub in TOC biogenesis: assembly is driven by TOC75 expression, with the Toc33and Toc159 GTPases being added sequentially thereafter. Integrative structural analysis revealed a modular architecture for TOC-P comprising a cytosolic GTPase receptor module linked flexibly to a membrane β-barrel channel module. TOC-N has a similar overall architecture, albeit with some clear differences that likely account for observed functional differences related to client 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