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Christina Stolze"],"technology_type":["Data-dependent acquisition","Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Arabidopsis thaliana","Stress-response","Plant growth","H2o2 homeostasis","Rcc1-like protein"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD073328"],"tissue":["Plant Cell"],"sample_protocol":["Affinity purification – mass spectrometry (AP–MS)  Approximately 15 g of freshly harvested leaf tissue per sample were ground in liquid nitrogen and extracted with 30 mL of lysis buffer (50 mM Tris-HCl [pH 7.5], 10% glycerol, 1 mM EDTA, 150 mM NaCl, 1% Triton X-100). The extracts were centrifuged at full speed (7,200 g) for 20 min at 4°C. From each sample’s supernatant, technical triplicates of 20 mg of total protein each were generated and adjusted to an equal volume of 10 mL in lysis buffer, and used for immunoprecipitation. The extracts were incubated for 1h at 4°C with 50 µL GFP-Trap® Agarose resin (ChromoTek), which had been prewashed three times with 1.5 mL extraction buffer and resuspended in 1000 µL lysis buffer before addition to the protein samples. The resins were pelleted at 500 rpm at 4°C and washed four times with 10 mL washing buffer (50 mM Tris–HCl [pH 7.5], 300 mM NaCl). Then, the resin was resuspended in 1 mL washing buffer, transferred to 1.5 mL Eppendorf tubes, and pelleted again. As controls, protein extracts were prepared in triplicate from wild type (Col) and Pro35S:StrepII-3xHA-YFP (Lapin et al, 2019) plants of the same age, harvested and processed in parallel with the ProUVR8:GFP-UVR8, Pro35S:CAIR1-YFP, Pro35S:YFP-CAIR1, ProCAIR1:CAIR1-GFP, and ProNCA1:NCA1-GFP samples. For GFP-CAT2 purification, the co-purifying proteins obtained with the peroxisomal marker line Pro35S:GFP-PTS1 (Mano et al, 2002) were included as additional control.  Sample preparation and LC-MS/MS data acquisition: Enriched proteins were submitted to an on-bead digestion using trypsin. In brief, dry beads were re-dissolved in 25 µL digestion buffer 1 (50 mM Tris, pH 7.5, 2M urea, 1mM DTT, 5 ng/µL trypsin) and incubated for 30 min at 32 °C in a Thermomixer with 400 rpm. Next, beads were pelleted and the supernatant was transferred to a fresh tube. Digestion buffer 2 (50 mM Tris, pH 7.5, 2M urea, 5 mM CAA) was added to the beads, after mixing the beads were pelleted, the supernatant was collected and combined with the previous one. The combined supernatants were then incubated o/n at 32 °C in a Thermomixer with 400 rpm; samples were protected from light during incubation. The digestion was stopped by adding 1 µL TFA and desalted with C18 Empore disk membranes according to the StageTip protocol (Rappsilber et al, 2003). Dried peptides were re-dissolved in 2% ACN, 0.1% TFA (10 µL) for analysis. Samples were analyzed using an EASY-nLC 1200 (Thermo Fisher) coupled to a Q Exactive Plus mass spectrometer (Thermo Fisher) or using an EASY-nLC 1000 (Thermo Fisher) coupled to a Q Exactive mass spectrometer (Thermo Fisher). Peptides were separated on 16 cm frit-less silica emitters (New Objective, 75 µm inner diameter), packed in-house with reversed-phase ReproSil-Pur C18 AQ 1.9 µm resin (Dr. Maisch, High Performance LC GmbH). Peptides were loaded on the column and eluted for 115 min using a segmented linear gradient of 5% to 95% solvent B (0 min : 5%B; 0-5 min -> 5%B; 5-65 min -> 20%B; 65-90 min ->35%B; 90-100 min -> 55%; 100-105 min ->95%, 105-115 min ->95%) (solvent A 0% ACN, 0.1% FA; solvent B 80% ACN, 0.1%FA) at a flow rate of 300 nL/min. Mass spectra were acquired in data-dependent acquisition mode with a TOP15 method. MS spectra were acquired in the Orbitrap analyzer with a mass range of 300–1750 m/z at a resolution of 70,000 FWHM and a target value of 3×106 ions. Precursors were selected with an isolation window of 1.3 m/z (Q Exactive Plus) or 2.0 m/z (Q Exactive). HCD fragmentation was performed at a normalized collision energy of 25. MS/MS spectra were acquired with a target value of 105 ions at a resolution of 17,500 FWHM, a maximum injection time (max.) of 55 ms and a fixed first mass of m/z 100. Peptides with a charge of +1, greater than 6, or with unassigned charge state were excluded from fragmentation for MS2, dynamic exclusion for 30s prevented repeated selection of precursors."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Alternatively, samples were analysed using an Ultimate 3000 RSLC nano (Thermo Fisher) coupled to an Orbitrap Exploris 480 mass spectrometer equipped with a FAIMS Pro interface for Field asymmetric ion mobility separation (Thermo Fisher). Peptides were pre-concentrated on an Acclaim PepMap 100 pre-column (75 µM x 2 cm, C18, 3 µM, 100 Å, Thermo Fisher) using the loading pump and buffer A** (water, 0.1% TFA) with a flow of 7 µl/min for 5 min. Peptides were separated on 16 cm frit-less silica emitters (New Objective, 75 µm inner diameter), packed in-house with reversed-phase ReproSil-Pur C18 AQ 1.9 µm resin (Dr. Maisch, High Performance LC GmbH). Peptides were loaded on the column and eluted for 130 min using a segmented linear gradient of 5% to 95% solvent B (0 min : 5%B; 0-5 min -> 5%B; 5-65 min -> 20%B; 65-90 min ->35%B; 90-100 min -> 55%; 100-105 min ->95%, 105-115 min ->95%, 115-115.1 min -> 5%, 115.1-130 min ->5%) (solvent A 0% ACN, 0.1% FA; solvent B 80% ACN, 0.1%FA) at a flow rate of 300 nL/min. Mass spectra were acquired in data-dependent acquisition mode with a TOP_S method using a cycle time of 2 seconds. For field asymmetric ion mobility separation (FAIMS) two compensation voltages (-45 and -60) were applied, the cycle time was set to 1 second for each experiment. MS spectra were acquired in the Orbitrap analyzer with a mass range of 320–1200 m/z at a resolution of 60,000 FWHM and a normalized AGC target of 300%. Precursors were filtered using the MIPS option (MIPS mode = peptide), the intensity threshold was set to 5000, Precursors were selected with an isolation window of 1.6 m/z. HCD fragmentation was performed at a normalized collision energy of 30%. MS/MS spectra were acquired with a target value of 75% ions at a resolution of 15,000 FWHM, inject time set to auto and a fixed first mass of m/z 120. Peptides with a charge of +1, greater than 6, or with unassigned charge state were excluded from fragmentation for MS2. Data analysis: Raw data were processed using MaxQuant software (version 1.6.3.4, http://www.maxquant.org/) (Cox & Mann, 2008) with label-free quantification (LFQ) and iBAQ enabled (Tyanova et al, 2016). MS/MS spectra were searched by the Andromeda search engine against a combined database containing the sequences from Arabidopsis (TAIR10_pep_20101214; ftp://ftp.arabidopsis.org/home/tair/Proteins/TAIR10_protein_lists/) and sequences of 248 common contaminant proteins and decoy sequences. Trypsin specificity was required and a maximum of two missed cleavages allowed. Minimal peptide length was set to seven amino acids. Carbamidomethylation of cysteine residues was set as fixed, oxidation of methionine and protein N-terminal acetylation as variable modifications. Peptide-spectrum-matches and proteins were retained if they were below a false discovery rate of 1%.  Statistical analysis of the MaxLFQ values was carried out using Perseus (version 1.5.8.5, http://www.maxquant.org/). Quantified proteins were filtered for reversehits and hits “identified by site”,  MaxLFQ values were log2 transformed. After grouping samples by condition only those proteins were retained for the subsequent analysis that had two valid values in one of the conditions. Two-sample t-tests were performed using a permutation-based FDR of 5%. Alternatively, quantified proteins were grouped by condition and only those hits were retained that had 3 valid values in one of the conditions. Missing values were imputed from a normal distribution (1.8 downshift, separately for each column). The Perseus output was exported and further processed using Excel. Candidates with LFQ intensity value > 20 and log2 ratio > 2 compared to both WT and “YFP” AP-controls were retained."],"omics_type":["Proteomics"],"labhead":["Hirofumi Nakagami"],"instrument_platform":[""],"labhead_affiliation":["Basic Immune System of Plants / Protein Mass Spectrometry Max Planck Institute for Plant Breeding Research Carl-von-Linne-Weg 10, 50829 Cologne, Germany"],"submission_type":["PARTIAL"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"submitter_mail":["stolze@mpipz.mpg.de"],"publication":["Not available"],"submitter_affiliation":["Plant Proteomics and Mass Spectrometry Group\nMax Planck Institute for Plant Breeding Research\nCarl-von-Linné Weg 10\n50829 Cologne"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"CATALASE INTERACTING RCC1-LIKE 1 contributes to hydrogen peroxide homeostasis in Arabidopsis","description":"Reactive oxygen species (ROS) are central regulators of plant growth and stress responses, and their cellular levels are tightly controlled by antioxidant systems, including the evolutionarily conserved catalases that decompose hydrogen peroxide (H2O2) predominantly within peroxisomes and glyoxysomes. Despite their importance, key aspects of catalase biogenesis, regulation, subcellular targeting, and potential extra-peroxisomal functions remain poorly understood. Using affinity purification of the UV-B photoreceptor UVR8 coupled with mass spectrometry, we identified a REGULATOR OF CHROMATIN CONDENSATION 1–like protein in Arabidopsis, which we named CATALASE-INTERACTING RCC1-LIKE 1 (CAIR1). CAIR1 interacts with all three catalase isoforms (CAT1–CAT3) as well as their chaperone NO CATALASE ACTIVITY 1 (NCA1). Loss-of-function cair1 mutants partially phenocopy cat2 and nca1, exhibiting reduced catalase activity, enhanced sensitivity to oxidative stress and alkaline growth conditions, and impaired primary root elongation. Mechanistically, cytosolic interaction between CAIR1 and CAT2 enhances total cellular catalase activity by facilitating peroxisomal import and proper subcellular localization of CAT2. In the absence of CAIR1, CAT2 forms aggregates, likely accounting for the observed loss of catalase activity. Notably, CAIR1 undergoes reversible, redox-dependent oligomerization that strengthens its interaction with catalases. Mutation of CAIR1 at Cys-356 and Cys-545 compromises this interaction under elevated ROS conditions and fails to rescue the oxidative stress sensitivity of cair1 mutants. Moreover, UV-B exposure suppresses catalase activity by weakening the interaction between CAIR1 and catalases, linking environmental light signaling to cellular redox regulation. Together, our findings reveal CAIR1 as a dynamic redox-responsive regulator of catalase activity that maintains cellular redox homeostasis by coordinating catalase localization and function through reversible oligomerization.","dates":{"publication":"2026-07-15","submission":"2026-01-21"},"accession":"PXD073328","cross_references":{"TAXONOMY":["NEWT:6945","NEWT:184922","NEWT:6703","NEWT:3555","NEWT:2","NEWT:157546","NEWT:35554","NEWT:38942","NEWT:307972","NEWT:32046","NEWT:544496","NEWT:2102","NEWT:2042546","NEWT:45351","NEWT:43179","NEWT:4513","NEWT:5722","NEWT:1247","NEWT:376741","NEWT:55153","NCBITaxon:10407","NEWT:1736309","NEWT:309800","NEWT:281395","NEWT:10360","NEWT:1211601","NEWT:876138","NEWT:47664","NEWT:3654","NEWT:237561","NEWT:5833","NEWT:6928","NEWT:10036","NEWT:36745","NEWT:498019","NEWT:1351","NEWT:1438992","NEWT:1352","NEWT:2649997","NEWT:272563","NEWT:224326","NCBITaxon:79857","NEWT:1096976","NEWT:82688","NEWT:95648","NEWT:3885","NEWT:3888","NEWT:5821","NEWT:1589","NEWT:135622","NCBITaxon:4896","NEWT:6915","NEWT:3649","NEWT:101510","NEWT:28903","NEWT:3880","NEWT:272559","NEWT:28909","NEWT:515849","NEWT:3641","NEWT:383379","NEWT:466585","NEWT:10029","NEWT:913645","NEWT:1000589","NEWT:85963","NEWT:85962","NEWT:143361","NEWT:317447","NEWT:7955","NEWT:7959","NEWT:2261","NEWT:31156","NEWT:398580","NEWT:4565","NEWT:1264690","NEWT:515619","NEWT:192875","NEWT:34305","NEWT:59729","NCBITaxon:183674","NEWT:224308","NEWT:84645","NEWT:626528","NEWT:3347","NEWT:139927","NEWT:4558","NEWT:209285","NEWT:5888","NEWT:211586","NEWT:747078","NEWT:1283","NEWT:931281","NEWT:4550","NEWT:1000561","NEWT:294381","NEWT:197","NEWT:1390363","NEWT:77133","NEWT:288705","NCBITaxon:79824","NEWT:4787","NCBITaxon:4563","NEWT:5755","NEWT:44689","NEWT:3218","NEWT:5759","NEWT:1736231","NEWT:1270","NEWT:374990","NEWT:498217","NEWT:156471","NEWT:2242","NEWT:4784","NEWT:11320","NEWT:360106","NEWT:156476","NEWT:286","NEWT:391619","NEWT:360104","NEWT:287","NEWT:246197","NEWT:10117","NEWT:10239","NEWT:10116","NEWT:1280","NEWT:1735272","NEWT:83334","NEWT:83332","NEWT:44685","NEWT:317513","NEWT:1148","NEWT:580240","NEWT:5508","NEWT:294128","NEWT:11676","NEWT:55571","NEWT:35500","NEWT:1140","NEWT:100226","NEWT:4530","NEWT:1143","NEWT:4896","NEWT:75058","NEWT:13616","NEWT:1390","NEWT:1094343","NEWT:1336795","NEWT:172","NEWT:296543","NEWT:316435","NEWT:1773","NEWT:1895","NEWT:1182590","NEWT:3712","NEWT:82380","NEWT:105023","NEWT:866628","NEWT:935293","NEWT:64152","NEWT:4924","NEWT:749200","NEWT:375146","NEWT:990346","NEWT:145953","NEWT:257309","NEWT:100816","NEWT:263","NEWT:230741","NEWT:52283","NEWT:284812","NCBITaxon:1313","NEWT:43330","NEWT:1603293","NEWT:408169","NEWT:44544","NEWT:47946","NEWT:4911","NEWT:645463","NEWT:3702","NEWT:129249","NEWT:243277","NEWT:990119","NEWT:2850","NEWT:408172","NEWT:408170","NEWT:493760","NEWT:106590","NEWT:260710","NEWT:257313","NEWT:400772","NEWT:3708","NEWT:128161","NEWT:332648","NEWT:106592","NEWT:536231","NEWT:1436733","NEWT:460519","NEWT:1187947","NEWT:1432138","NEWT:269796","NEWT:10312","NEWT:1424507","NCBITaxon:1773","NEWT:9598","NEWT:8030","NEWT:9483","NEWT:1639","NEWT:188229","NEWT:3818","NEWT:480","NEWT:4909","NEWT:67767","NEWT:432359","NEWT:46835","NEWT:1182263","NEWT:109757","NEWT:943146","NEWT:2711","NEWT:300852","NEWT:1502","NEWT:376686","NEWT:95486","NEWT:9103","NEWT:1883446","NEWT:29159","NEWT:253","NEWT:10306","NCBITaxon:2759","NEWT:1233435","NEWT:93061","NEWT:8022","NEWT:145943","NCBITaxon:4932","NEWT:595536","NEWT:240906","NEWT:593117","NEWT:89920","NEWT:3635","NEWT:5811","NEWT:235443","NEWT:180923","NEWT:108458","NEWT:272623","NEWT:272624","NEWT:411483","NEWT:884019","NEWT:198215","NEWT:411490","NEWT:983964","NEWT:118499","NEWT:169963","NEWT:32644","NEWT:527796","NEWT:225117","NEWT:499175","NEWT:109779","NEWT:476272","NEWT:3747","NEWT:195051","NEWT:367830","NEWT:1255228","NEWT:178616","NEWT:649908","NEWT:410289","NEWT:373153","NEWT:375451","NEWT:352472","NEWT:357","NEWT:1071661","NEWT:360094","NEWT:470","NEWT:41364","NEWT:1313","NEWT:411469","NEWT:84023","NEWT:559292","NEWT:39491","NCBITaxon:5811","NEWT:411464","NEWT:411460","NEWT:2014887","NEWT:2762","NEWT:1174673","NEWT:1328426","NEWT:562","NEWT:411470","NEWT:33952","NEWT:2094720","NCBITaxon:2697049","NEWT:571256","NEWT:28038","NEWT:1663","NEWT:1423","NEWT:4932","NEWT:3603","NEWT:2759","NEWT:3847","NEWT:38293","NEWT:327159","NEWT:178876","NEWT:1660","NEWT:327160","NEWT:573","NEWT:9031","NEWT:1872122","NEWT:7091","NEWT:108931","NEWT:241368","NEWT:42528","NEWT:190802","NEWT:9778","NEWT:150475","NEWT:303","NEWT:9417","NEWT:7111","NEWT:347515","NEWT:1216979","NEWT:7237","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:115104","NEWT:1121114","NEWT:663","NEWT:1081927","NEWT:1238993","NEWT:67825","NEWT:185579","NEWT:941442","NEWT:220668","NEWT:13076","NEWT:1821314","NEWT:1249668","NEWT:7108","NEWT:317","NEWT:5286","NEWT:7227","NEWT:7469","NEWT:885318","NEWT:9402","NEWT:9644","NEWT:415540","NEWT:550","NEWT:675060","NEWT:4081","NEWT:334542","NEWT:554","NEWT:27592","NEWT:98334","NEWT:426428","NEWT:63459","NEWT:1276815","NEWT:36185","NEWT:588858","NEWT:9639","NCBITaxon:11071","NEWT:242231","NEWT:7574","NEWT:1715256","NEWT:7215","NEWT:575412","NEWT:929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