{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/File_List.xlsx"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/hf2023021310.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/hf2023021314.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/hf2023021302.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/hf2023021306.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/hf2023021334.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/hf2023021322.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/hf2023021326.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/hf2023021318.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/hf2023021330.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/tabacum_wtFBN1.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/Ntabacum_cTP.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/tabacum_FBN1a17Dalpha.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/cTP.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/MaxQuant_v2.4.5.0.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/FBN1a17alpha.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD045458/WtFBN1a.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["pklundqu@msu.edu"],"submitter":["Peter Lundquist"],"technology_type":["Mass Spectrometry","Shotgun proteomics"],"software":[""],"submitter_keywords":["Tobacco","Plastoglobule","Fibrillin"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD045458"],"sample_protocol":["Plastoglobules were isolated from total leaf tissue according to the protocol described in Espinoza-Corral, et al. The Plant Journal (2021), lyophilized and stored at -80C until LC-MS/MS analysis. Lyophilized samples were re-suspended in 50 µL of 125 mM Tris, pH 6.8, 4% SDS, 20% glycerol, heated to 600C for 5 min and electrophoresed into a 12% Tris-HCl Criterion gel from BioRad at 50V for ~20 min or until the dye front moved just below the bottom of the sample wells. Electrophoresis was stopped and the gel stained with Coomassie Blue protein stain until bands appeared. Protein bands were excised from the gel and digested according to Shevchenko, et. al. with modifications. Briefly, gel bands were dehydrated using 100% acetonitrile and incubated with 10mM dithiothreitol in 100 mM ammonium bicarbonate, pH~8, at 560C for 45 min, dehydrated again and incubated in the dark with 50 mM iodoacetamide in 100 mM ammonium bicarbonate for 20 min. Gel bands were then washed with ammonium bicarbonate and dehydrated again. Sequencing grade modified trypsin was prepared to 0.01 µg/µL in 50 mM ammonium bicarbonate and ~100 uL of this was added to each gel band so that the gel was completely submerged. Bands were then incubated at 370C overnight. Peptides were extracted from the gel by water bath sonication in a solution of 60% Acetonitrile (ACN) /1% Trifluoroacetic acid (TFA) and vacuum dried to ~2 µL. Injections of 5 µL were automatically made using a Thermo (www.thermo.com) EASYnLC 1200 onto a Thermo Acclaim PepMap RSLC 0.1mm x 20mm C18 trapping column and washed for ~5 min with Buffer A. Bound peptides were then eluted over 65 min onto a Thermo Acclaim PepMap RSLC 0.075 mm x 500 mm resolving column with a gradient of 8% B to 40% B in 54 min, ramping to 90% B at 55 min and held at 90% B for the duration of the run (Buffer A = 99.9% Water/0.1% Formic Acid, Buffer B = 80% Acetonitrile/0.1% Formic Acid/19.9% Water) at a constant flow rate of 300 nL/min. Column temperature was maintained at a constant temperature of 50oC using and integrated column oven (PRSO-V2, Sonation GmbH, Biberach, Germany). Eluted peptides were sprayed into a ThermoScientific Q-Exactive HF-X mass spectrometer (www.thermo.com) using a FlexSpray spray ion source. Survey scans were taken in the Orbitrap (60000 resolution, determined at m/z 200) and the top 15 ions in each survey scan were then subjected to automatic higher energy collision induced dissociation (HCD) with fragment spectra acquired at 7,500 resolution."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The resulting MS/MS spectra were converted to peak lists using MaxQuant v2.4.5.0 and searched against a protein database using the Andromeda search algorithm, a part of the MaxQuant environment (83, 84). LC-MS/MS .raw files from samples expressing each protein variant were searched separately using a protein database containing all N. tabacum protein sequences available from UniProt (https://www.uniprot.org/uniprotkb?query=nicotiana+tabacum; 82358 proteins) with common laboratory contaminants and the respective AtFBN protein sequence appended. Oxidation of methionine, deamidation of asparagine, and N-terminal and lysine acetylation were set as variable modifications; carbamidomethylation was set as a fixed modification. Digestion mode was trypsin/P with a maximum of two missed cleavages. MS/MS tolerance of the first search was 20 ppm, and the main search was 4.5 ppm, with individualized peptide mass tolerance selected. FDR at peptide spectrum match and protein levels was set as 0.01, estimated using the reverse decoy method (85). LFQ intensity was determined as the total sum of the peak of Unique and Razor peptides with Fast LFQ selected. The best gene model for each protein group was identified as that with the highest number of Unique + Razor Peptide counts when compiled across all experiments. In the case of a tie, the lowest gene model number was selected, regardless of whether the protein group contained gene models from one or more gene loci."],"omics_type":["Proteomics"],"labhead":["Peter K Lundquist"],"instrument_platform":[""],"labhead_affiliation":["Michigan State University, Biochemical & Molecular Biology Department and Plant Resilience Institute"],"submission_type":["PARTIAL"],"species":["Nicotiana Tabacum (common Tobacco)","Arabidopsis Thaliana (mouse-ear Cress)"],"submitter_mail":["pklundqu@msu.edu"],"publication":["10.1093/PCP/PCAG047"],"submitter_affiliation":["Michigan State University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"N. benthamiana Plastoglobule Proteome","description":"Plant chloroplasts contain ubiquitous lipid droplets known as plastoglobules which are characterized by a galactolipid monolayer surrounding a neutral lipid core. Plastoglobules are implicated in plant development and stress tolerance and harbor a set of approximately 30 proteins that presumably drive plastoglobule function. Due to the monolayer structure of plastoglobules, these proteins must associate peripherally. However, targeting determinants have not been identified among any plastoglobule protein, and the protein-membrane interaction mechanisms that establish the plastoglobule proteome remain unclear. We demonstrate that plastoglobule-localized Fibrillins harbor an amphipathic helix at the lip of their β-barrel structure that is necessary for proper plastoglobule association. This project sought to test the impacts of heterologous ectopic targeting of the Arabidopsis thaliana Fibrillin 1a on the tobacco (N. benthamiana) plastoglobule proteome. AtFBN1a, and a deletion-variants removing the amphipathic helix were transiently transformed into tobacco leaf tissue. Isolated plastoglobules were subjected to bottom-up shotgun proteomics analysis with label-free quantification. Isolated plastoglobules from tobacco transiently transformed with GFP alone, driven to the chloroplast stroma by the Rubisco chloroplast transit peptide, were also analyzed as a negative control. The quantitative N. benthamiana plastoglobule proteome from the negative control plants was established, representing the baseline tobacco plastoglobule proteome. This revealed a proteome rich in Fibrillins, representing approximately 66% of the total protein mass, as well as many ABC1 kinases, and lipid metabolic enzymes, similar to the proteome of Arabidopsis. In the presence of ectopic AtFBN proteins, certain proteins were found to be reduced or increased in abundance, pointing to candidate proteins that are either outcompeted from the plastoglobule surface by AtFBN1a or recruited to the plastoglobule by 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