{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067053/P336_01_experimentalDesignTemplate.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067053/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067053/BBM_815_P336_01_FRH_009.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067053/BBM_815_P336_01_FRH_004.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067053/BBM_815_P336_01_FRH_010.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067053/BBM_815_P336_01_FRH_003.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067053/BBM_815_P336_01_FRH_013.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067053/BBM_815_P336_01_FRH_001.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067053/TAIR10_pep_20101214_updated.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD067053/P336_01_CesET_CesAA_MaxQuant_results.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["tina.ludwig@tum.de"],"submitter":["Christina Ludwig"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Brassinosteroid","Bhlh proteins","Epigenetics","Biotic stress","Nlrs","Steroids"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067053"],"tissue":["Seedling"],"sample_protocol":["Seeds of the lines 35S:CESwt-YFP/32 and 35S:CESS75A+S77A-YFP/310 22,23 were germinated on ½ MS medium and after 10 days approximately 2 g of plant tissue per line were harvested and  ground to a fine powder in liquid nitrogen. The powder was resuspended in 6 ml of lysis buffer (50 mM Tris/HCl pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10% glycerol, 1 mM EDTA, 5 mM DTT, 0.2% NonidetTM P-40, 1 mM PMSF, 1x protease inhibitor cocktail), vortexed for 1 min and incubated on ice for 30 min. Cell lysates were centrifuged at 2,000 × g for 15 min at 4 °C, and the cleared supernatant was collected. Total protein concentration was determined using the Bradford Assay. 50 μl GFP-Trap agarose beads (ChromoTek) were prewashed with 500 μl of lysis buffer and incubated with supernatant containing 5 mg of total protein at 4 °C for 2 h with gentle rotation. Beads were then pelleted by centrifugation at 2,500 × g for 5 min at 4 °C, and the supernatant was discarded. The beads were washed twice with 500 μl of lysis buffer, were resuspended in 80 μl of 2x SDS-sample buffer (120 mM Tris/HCl pH 6.8, 20% glycerol, 4 % SDS, 0.04% bromophenol blue, 10% 2-mercaptoethanol) and boiled at 95 °C for 5 min. The supernatant was collected after centrifugation and subjected to mass spectrometry analysis. In‐gel trypsin digestion was performed according to standard procedures (Shevchenko et al., 2006). Briefly, samples were run on a Nu-PAGE™ 4%–12% Bis‐Tris protein gel (ThermoFisher Scientific) for about 1 cm and the not size‐separated protein band was cut out, reduced (10 mM dithiothreitol in 5 mM TEAB), alkylated (55 mM chloroacetamide in 5 mM TEAB) and digested overnight with trypsin (Trypsin Gold, mass spectrometry grade, Promega). The peptides obtained were dried to completeness and resuspended in 12 μL of 2% acetonitrile, 0.1% formic acid in HPLC grade water. 5 μL sample were injected per mass spectrometric (MS) measurement."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["LC-MS/MS data acquisition was carried out on a Dionex Ultimate 3000 RSLCnano system coupled to an Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific). Injected peptides were delivered to a trap column (ReproSil-pur C18-AQ, 5 μm, Dr. Maisch, 20 mm × 75 μm, self-packed) at a flow rate of 5 μL/min in 0.1% formic acid in HPLC grade water. After 10 minutes of loading, peptides were transferred to an analytical column (ReproSil Gold C18-AQ, 3 μm, Dr. Maisch, 450 mm × 75 μm, self-packed), and separated using a 50 min gradient from 4% to 32% of solvent B (0.1% FA, 5% DMSO in acetonitrile) in solvent A (0.1% FA, 5% DMSO in HPLC grade water) at 300 nL/min flow rate. The mass spectrometer was operated in data-dependent acquisition (DDA) and positive ionization mode. MS1 spectra (360–1300 m/z) were recorded at a resolution of 60k using a normalized automatic gain control (AGC) target value of 100% and a maximum injection time (maxIT) of 50 msec. A cycle time of 2 sec was set. Only precursors with charge states 2 to 6 were selected, and dynamic exclusion of 30 sec was enabled. Peptide fragmentation was performed using higher energy collision-induced dissociation (HCD) and a normalized collision energy (NCE) of 30%. The precursor isolation window width was set to 1.3 m/z. MS2 Resolution was 15.000 with a normalized automatic gain control (AGC) target value of 150% and maximum injection time (maxIT) of 22 msec.  Peptide identification and quantification was performed using the software MaxQuant (version 1.6.3.4). MS2 spectra were searched against the Arabidopsis thaliana protein database from the Arabidopsis Information Resource (TAIR) (35,386 protein entries), supplemented with common contaminants (built‐in option in MaxQuant). Trypsin/P was specified as proteolytic enzyme. Carbamidomethylated cysteine was set as fixed modification. Oxidation of methionine and acetylation at the protein N‐terminus was specified as variable modifications. Results were adjusted to 1% false discovery rate on peptide spectrum match (PSM) and protein level employing a target‐decoy approach using reversed protein sequences. Label-Free Quantification (LFQ) was used for protein quantification with at least 2 peptides per protein. The minimal peptide length was defined as 7 amino acids and the “match-between-runs” functionality was disabled.  Protein results were further processed and visualized using the platform omicsViewer (DOI: 10.1101/2022.03.10.483845). Proteins were filtered for at least two valid quantification values over the three replicate measurements of either CESwt  or CESAA. Missing values were imputed as half the lowest detected LFQ intensity per protein, unless the imputed value exceeded the sample's 15th percentile, in which case the 15th percentile value was imputed. Differential protein expression between two strains was determined through Student t-test. The resulting p-values were adjusted by the Benjamini-Hochberg algorithm to control the false discovery rate. Only proteins with a fold change of ≥ 2 and an adjusted p-value < 0.05 were considered significant."],"omics_type":["Proteomics"],"labhead":["Christina Ludwig"],"instrument_platform":[""],"labhead_affiliation":["Bavarian Center for Biomolecular Mass Spectrometry (BayBioMS) Technical University of Munich (TUM) Gregor-Mendel-Strasse 4 85354 Freising Germany"],"submission_type":["PARTIAL"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"submitter_mail":["tina.ludwig@tum.de"],"publication":["Not available"],"submitter_affiliation":["TU Munich"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Brassinosteroid-regulated transcription factors confer epigenetic changes that repress plant immunity","description":"When organisms encounter pathogens, they rapidly activate complex defense programs to ensure survival. While these immune responses are vital, they often also incur trade-offs, such as reduced growth and development and must therefore be tightly controlled. In this study, we reveal that the steroid hormones brassinosteroids (BRs) contribute to this control in Arabidopsis thaliana by repressing immunity-related genes. We provide evidence that the BR-regulated basic helix-loop-helix (bHLH) transcription factor CESTA (CES), along with its homologs BR ENHANCED EXPRESSION (BEE)1-3, mediate DNA methylation changes at transposable element (TE)-rich loci containing nucleotide-binding leucine-rich-repeat (NLR)-type receptor genes, including SUPPRESSOR OF NPR1-1 CONSTITUTIVE 1 (SNC1). These CES-induced methylation changes correlate with altered splicing of SNC1 pre-mRNA, a process that requires the BR receptor BRASSINOSTEROID INSENSITIVE 1 (BRI1). In support, we show that CES associates with components of the chromatin remodeling and splicing machinery. Together, our findings reveal a previously unrecognized BR-induced mechanism that modulates the epigenetic and post transcriptional regulation of immune genes, enabling plants to prioritize growth over defense. 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