{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_C5_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_C6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_C6_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_D3_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190708_24_MS19-164_Leaf_C5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_C4_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190708_24_MS19-164_Leaf_C6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_D1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190718_24_MS19-164_Leaf_C5_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190708_24_MS19-164_Leaf_D2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190718_24_MS19-164_Leaf_C4_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_D2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_C4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190708_24_MS19-164_Leaf_D1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_D2_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190708_24_MS19-164_Leaf_D3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190718_24_MS19-164_Leaf_D2_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190718_24_MS19-164_Leaf_D1_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_D1_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190718_24_MS19-164_Leaf_D3_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_D3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190718_24_MS19-164_Leaf_C6_Phospho.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190708_24_MS19-164_Leaf_C4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/OT_190809_25_MS19-191_Silk_C5.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/uniprotkb_maize_B73_2024_12_20.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/Maize_Silk_Phos_txt.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/Maize_Leaf_LFQ_txt.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/Maize_Leaf_Phos_txt.7z","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD061787/Maize_Silk_LFQ_txt.7z"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["alex.jones@warwick.ac.uk"],"submitter":["Georgina Charlton"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Disease Free"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD061787"],"tissue":["Leaf","Corn Silk"],"sample_protocol":["2.2. Protein ExtractionMaize leaves and maize silks were ground in liquid nitrogen to a fine powder. Buffer (PBS, 500 mM sucrose, 10% glycerol, 20 mM ethylenediaminetetraacetic acid (EDTA), 20 mM ethylene glycol-bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid (EGTA), 50 mM sodium fluoride (NaF), 5 mM β-glycerophosphate, 0.6% polyvinylpyr-rolidone (PVP), 10 mM ascorbic acid, 1 mM phenylmethylsulfonyl fluoride (PMSF), 1 mM dithiothreitol (DTT), 1× protease inhibitor cocktail (PIC) (AMS-BIO, Cambridge, UK)) was added and samples were vortexed and fil-tered through Miracloth (Merck, Darmstadt, Germany). Samples were then centrifuged at 20,000× g for 30 min at 4 °C. Protein concentration was established using a Bradford assay and protein quality was checked by running 20 µg of protein on a 12% SDS-PAGE gel.2.3. Filter-Aided Sample Preparation DigestProtein samples at 1 mg/mL in PBS pH 7.4 were transferred into 0.5 mL 10 kDa cut off filter columns (Millipore, Glasgow, UK) and spun at 8000× g for 20 min. Samples were washed 3 times with 6 M urea (MerckSigma Aldrich), centrifuging at 8000× g for 20 min each time. Samples were washed 3 times with 50 mM ABC. Samples were incubated with 10 mM Tris(2-carboxyethyl)phosphine (TCEP) (Sigma Aldrich) and 40 mM Chloroa-cetamide (CAA) (Sigma Aldrich) to reduce disulphide bonds and alkylate cysteines, for 30 min at room temperature. TCEP- and CAA-treated samples were spun through the filter at 8000× g for 20 min. The filter was washed 3 times with 50 mM HEPES. A total of 1 µg of trypsin (Promega, Southampton, UK) per 100 µg of protein was added, and sam-ples were left digesting overnight at 37 °C. The peptides were then centrifuged through the filter column for 20 min at 8000× g. The filter was washed with water to collect any residual peptides left on the filter. Peptides were desalted using C18 reverse phase tips before removal of acetonitrile using a Concentrator Plus Speed Vac (Eppendorf, Leipzig, Germany).2.4. Phosphopeptide EnrichmentAfter filter-aided sample preparation (FASP) digestion phosphopeptides were en-riched using Titanospere titanium dioxide (TiO2) beads (GL Sciences Inc. Tokyo Japan). Peptides in 50 mM HEPES were diluted to 5 mM HEPES with 80% acetonitrile (AcN) and 5% TFA. TiO2 beads were diluted to 1 mg in 10 µL of 2,5-dihydroxybenzoic acid (DHB) (Sigma AldrichMerk) solution at 20 mg/mL and mixed for 10 min at 650 rpm. In total, 2 mg of beads were added for every 1 mg of peptides and were mixed gently with end-over-end mixing for 1 h. This was repeated once. Beads were centrifuged at 2000× g for 2 min and the supernatant was removed. A C8 membrane was packed into a 200 µL pipette tip to make a column to support the beads. The beads were added on top of the C8 membrane and washed with 10% AcNcan; this was centrifuged through at 2000× g for 10 min. Beads were then washed with 40% AcN and spun at 2000× g for 6 min. Beads were finally washed with 60% AcN and spun at 2000× g for 4 min. Peptides were eluted from the beads using 5% ammonium hydroxide (Sigma AldrichMerk) followed by 15% ammonium hydroxide, 25% AcN and centrifuged at 2000× g for 2 min. The ammonium hydroxide and AcN were removed by speed vac for 20 min. Samples were resuspended in 2% AcN 0.1% TFA and sonicated for 15 min before the clean up via C18 stage tip.2.5. For All Proteomic AnalysisPeptide mixtures were resuspended in 2%  AcNacetonitrile, 0.1% TFA and were analysed by nano-LC-MS/MS using an Ultimate3000 high-performance liquid chroma-tography system coupled online to an Orbitrap Fusion Tribrid mass spectrometer (Thermo Fisher Scientific, Loughborough UK). Buffer A consisted of water acidified with 0.1%  TFAformic acid, while buffer B consisted of acetonitrile with 0.1% TFA formic acid and samples were run on a 45 min LC gradient. The peptides were first trapped for 5 min at 10 μL/min with 96% buffer A on a trap (Acclaim PepMap µ-precolumn cartridge 300 µm i.d. × 5 mm, 5 μm 100 Å; (Thermo Scientific, Loughborough UK); after trapping, the peptides were separated by a 50 cm analytical column (Acclaim PepMap RSLC 75 µm i.d. × 50 cm, 2 µm, 100 Å; Thermo Fisher Scientific). To avoid cross-contamination be-tween samples, a wash of 30 min was run between biological replicates (one technical replicate was performed for each sample).Peptides were ionised using a spray voltage of 2.1 kV and a capillary heated at 275 °C. The mass spectrometer was set to acquire full-scan MS spectra (375 to 1575 m/z) for a maximum injection time set to 150 ms at a mass resolution of 120,000 and an automated gain control (AGC) target value set to 500,000. Accurate mass measurements were made using data-dependent acquisition (DDA). The most intense precursors with charge states between +2 and +6 were selected for fragmentation. HCD fragmentation was performed in the HCD cell, with the readout in the Ion Trap mass analyser (isolation window of 1.2 m/z) and an AGC target value of 5000 with a maximum injection time set to 200 ms and a normalised collision energy of 33%.2.6. Maize Leaf Global Proteomic AnalysisThe gradient was 8% to 35% B in 24 min at 250 nL/min. Buffer B was then increased to 80% for the cleaning step. Dynamic exclusion was used with a 20 s window to prevent repeated selection of peptides.2.7. Maize Silk Global Proteomic AnalysisThe gradient was 8% to 25% B in 82 min at 250 nL/min. Buffer B was then raised to 35% in 9 min and increased to 90% for the cleaning step. Dynamic exclusion was used with a 45 s window to prevent repeated selection of peptides.2.8. Phosphopeptide DetectionThe gradient was 6% to 25% B in 31 min at 250 nL/min. Buffer B was then raised to 37% in 10 min and increased to 80% for the cleaning step. Dynamic exclusion was used with a 25 s window to prevent repeated selection of peptides."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Peptide Assignment and Label-Free Quantification Using Max QuantXcalibur RAW files were analysed using Max Quant (MQ) version 2.6.6.0. Sam-ples were searched using the Uniprot Zea mays UNIPROT database consisting of 148,866 protein sequences downloaded on 20th December 2024 (https://www.uniprot.org/uniprotkb?query=maize+B73). Trypsin was set as the digestion enzyme, with up to 2 missed cleavages, and a parent ion mass tolerance of 4.5 ppm. Oxidation of Met was set as a variable modification and Carbamidomethyl of Cys as a fixed modification for all searches. For phosphopeptide enrichments, phos-phorylation on S, T, and Y was set as a variable modification. Label-free quantification (LFQ) was used for quantification and the match between runs was used.The protein groups text file from the MQ search was loaded into Perseus, and LFQ intensities for each sample were loaded into the main column. Potential contaminant hits, only identified by site, reverse database and single peptide hits, were filtered out of the data. The data was transformed log2X and samples were grouped into treated and control. Proteins with missing values in at least 1 out of 3 reps in one group were removed from the dataset and missing values were replaced from the normal distribution. PCA plots, and volcano plots and heat maps could then be generated.The phospho (STY) sites text file from the MQ search was loaded into Perseus, and intensity 1, 2 and 3 for each sample was loaded into the main column. Potential contaminant hits and reverse database hits were filtered out of the data. The modification table was expanded, samples were grouped into treated and control, and the data was transformed log2X. Peptides with missing values of more than 1 out of 3 reps in one group were removed from the dataset and other missing values were replaced from the normal distribution. PCA plots, and volcano plots and heat maps could then be gener-ated."],"omics_type":["Proteomics"],"labhead":["Alex Jones"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["School of Life Sciences, University of Warwick"],"species":["Zea Mays (maize)"],"publication":["10.3390/PROTEOMES14020025"],"submitter_mail":["georgina.charlton@ucl.ac.uk"],"submitter_affiliation":["University College London"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Changes in the Proteome and Phosphoproteome of Zea mays Tissues in Drought Stress Show Plant Tissue Re-sponses from Dehydrins, Carboxylic Acid Metabolism, RNA Splicing and Transcription Factors","description":"Background: Maize is a vital crop, supporting 19.5% of global calorie intake. However, maize is vulnerable to even brief periods of drought which substantially re-duces seed set and therefore yield. Methods: To identify proteins involved in responses of maize to drought, soluble proteins were extracted from leaf and silk tissues of Zea mays and protein abundance and phosphorylation status were quantified relative to well-watered controls. Label-free quantification and phosphopeptide enrichment were applied to the same biological samples and over 300 proteins were identified with sig-nificantly different changes. Results: Proteins known to be involved in drought responses were identified, such as the abscisic acid pathway and transcription factors. Of particular interest is a group of dehydrins quantified at both total protein and phosphopeptide levels, permitting insight into stoichiometry. The biological function of dehydrins in the model plant Arabidopsis thaliana is known to be regulated by phosphorylation. Conclu-sions: Translation of protein function from model plant to crops remains highly chal-lenging because genome duplication has created complex sets of orthologous and ho-mologous proteins. By focusing on proteomic changes during crop stress responses, this work enables the identification of known and novel proteins, substantially aiding the transfer of knowledge from model plants to crops.","dates":{"publication":"2026-05-15","submission":"2025-03-13"},"accession":"PXD061787","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:193528","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","NEWT:156563","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:10031","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:1190602","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:1176302","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:143292","NEWT:2767842","NEWT:314345","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","NCBITaxon:77643","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:1072569","NEWT:1072568","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1336794","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3710","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:32201","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:10882","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3707","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:223074","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2422","NEWT:2423","NEWT:3755","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:1195466","NEWT:85698","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:427924","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:1120755","NEWT:1862567","NEWT:591090","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:29471","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:550","NEWT:10804","NEWT:52694","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:366497","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:771875","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:480020","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:518","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:7375","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639",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