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GietlerMass SpectrometryTop-down proteomicsSolanum tuberosum l.Protein carbonylationElevated temperatureDrought stresshttps://www.ebi.ac.uk/pride/archive/projects/PXD075691LeafProtein carbonylation was determined according to Levine et al. (1994) [41] using DNPH (2,4-dinitrophenylhydrazine) derivatization. The absorbance was measured at 375 nm, and results were expressed as nmol carbonyl per mg of protein. The 20S proteasome activity was measured fluorometrically using 5 µg of total protein with a commercial as-say kit (MAK172, Sigma-Aldrich), following the manufacturer’s instructions. Total Protein Extraction. Leaf tissue (150 mg) was ground in liquid nitrogen, and proteins were precipitated with ice-cold 10% TCA/acetone. The resulting pellet washed sequentially with 10% TCA/acetone, 80% methanol containing 0.1 M ammonium acetate, and 80% acetone. The dried pellet was resuspended in a mixture of Tris-buffered phenol (pH 8.0) and SDS extraction buffer (0.1 M Tris-HCl, 30% sucrose, 5% β-mercaptoethanol, 2% SDS). After centrifugation, the phenolic phase was collected. Proteins were precipitated overnight with 0.1 M ammonium acetate in 80% methanol at −20 °C, washed with meth-anol and acetone, and finally dissolved in IEF buffer (7 M urea, 2 M thiourea, 4% CHAPS, 40 mM DTT). Protein concentration was determined using the Bradford-based method adapted for proteomic samples [42]. Two-Dimensional Gel Electrophoresis (2D-PAGE) and Immunoblotting. For proteo-me mapping, 120 µg of protein was loaded onto 7-cm pH 4–7 NL Immobiline DryStrips. Following isoelectric focusing (IEF), strips were equilibrated in buffers containing DTT (reduction) and iodoacetamide (alkylation) and separated on 11% SDS-PAGE gels. Gels were stained with colloidal Coomassie Brilliant Blue G-250. For carbonylation detection, 20 µg of protein was derivatized with DNPH before IEF. After 2D separation, proteins were electro-transferred to PVDF membranes. Membranes were blocked with 5% non-fat milk and incubated with primary anti-DNP antibodies (Sigma-Aldrich), followed by alkaline phosphatase-conjugated secondary antibodies. Signals were visualized using NBT/BCIP substrate and the reaction was terminated with distilled water. Four biological replicates were conducted for each experimental variant, including protein purification, two-dimensional electrophoresis (2DE), membrane transfer, and immunochemical staining (n = 4). Gels and PVDF membranes were scanned using an Image Scanner III (GE Healthcare), and their digital images were analyzed with Delta2D Version 2.0 software (DECODON GmbH, Greifswald, Germany). Differential proteins were identified by comparing plants subjected to drought, high temperature, and a combination of these stresses with control leaves from the same cul-ti-var. After correcting for positional spot variations, a virtual fused image was created to consolidate the information from all images into one composite image, followed by the detection of a consensus spot pattern. For spot quantification based on size and intensity, a standard procedure embedded in the software was applied to all membrane images from the experiment. Normalized spot intensities were calculated by relating the intensity of each in-di-vidual spot to the total intensity of all detected spots in the gel or membrane image. The accuracy of gel or membrane identity between biological replicates was assessed using principal component analysis (PCA), which served as both a quality control step and a means of comparing all experimental variants. The selection of differential proteins was based on mean spot intensity and was evaluated using one-way ANOVA with an ad-just-ed Bonferroni correction (critical p-value < 0.01). Images of selected spots on mem-branes were overlaid onto the corresponding gel images, and the selected spots were then excised from the gels for identification purposes.PrideNot availableDifferential spots were excised, destained, and subjected to in-gel trypsin digestion. Peptides were analyzed by LC–MS/MS using an Orbitrap Exploris 480 (Thermo Fisher Scientific). MS/MS spectra were searched against the Solanum tuberosum NCBI database using the MASCOT engine. Search parameters included: ±5 ppm peptide tolerance, ±0.01 Da fragment tolerance, and two missed cleavages. Carbamidomethylation was set as a fixed modification, while methionine oxidation was considered a variable modification.ProteomicsMarta GietlerDepartment of Biochemistry and Microbiology, Institute of Biology, Warsaw University of Life Scienc-es-SGGW, PolandCOMPLETESolanum Tuberosum (potato)marta_gietler@sggw.edu.pl41901459 Boguszewska-Mańkowska D, Fidler-Jarkowska J, Gietler M, Nykiel M. Stress-Specific Carbonylation and Proteasome 20S Activity in Potato Under Drought, Elevated Temperature, and Combined Stresses: Linking Oxidative Damage to Proteome Regulation. Plants (Basel). 2026 15(6):939 10.3390/plants15060939Department of Biochemistry and Microbiology, Institute of Biology, Warsaw University of Life Sciences‐SGGW, Warsaw, PolandPoland10.6019/PXD075691Drought and elevated temperature are major abiotic stresses that limit potato growth and productivity; however, their combined effects on biomass and oxidative damage to proteins remain poorly understood. We investigated individual and interactive effects of drought and elevated temperature on growth traits, yield, protein carbonylation, 20S proteasome activity, and the leaf proteome. Results show that while an elevated temperature alone did not significantly impair vegetative biomass or yield, it markedly intensified the negative impacts of drought during simultaneous exposure. Drought and combined stress substantially reduced stem and leaf mass, as well as assimilation area. Biochemically, drought induced protein carbonylation and stimulated 20S proteasome activity. Interestingly, elevated temperature reduced carbonylation and proteasome activity, yet its presence in combined stress exacerbated oxidative damage compared to drought. Proteomic analysis revealed stress-specific carbonylation of molecular chaperones, antioxidant enzymes, and proteins involved in photosynthesis, glycolysis, and energy metabolism. These results suggest that while potato plants exhibit resilience to moderately elevated temperature, the synergistic effect of heat and drought triggers a more severe oxidative challenge. This requires enhanced proteolytic and antioxidant mechanisms to maintain growth and productivity under complex stress conditions.Stress-Specific Carbonylation and Proteasome 20S Activity in Potato Under Drought, Elevated Temperature, and Combined Stresses: Linking Oxidative Damage to Proteome Regulation.Boguszewska-Mańkowska Dominika D, Fidler-Jarkowska Justyna J, Gietler Marta M, Nykiel Małgorzata MfalseStress-Specific Carbonylation and Proteasome 20S Activity in Potato under Drought, Elevated Temperature, and Combined Stresses: Linking Oxidative Damage to Proteome RegulationThis study investigates stress-specific patterns of protein carbonylation and proteome re-modelling in potato leaves subjected to drought, elevated temperature, and their combina-tion. The research was conducted at the Department of Potato Agronomy of the Plant Breeding and Acclimatization Institute – National Research Institute. The Polish potato cultivar Solanum tuberosum L. ‘Lech’, known for its sensitivity to soil drought, was used in the study.Two weeks after tuber initiation (approximately BBCH 40), plants were subjected to four experimental treatments for a duration of 14 days: Control (C): maintained optimal hydration (70% field water capacity, FWC) and standard temperature conditions (20/16°C day/night). Drought (D): water withheld to reach and maintain 40% FWC at 20/16°C. Elevated Temperature (HT): plants exposed to 38/25°C (day/night) under optimal hydration (70% FWC). Combined Stress (D+HT): plants exposed to 38/25°C (day/night) with water withheld to 40% FWC.2026-04-062026-03-16PXD075691NEWT:1773NEWT:6945NEWT:3555NEWT:38783NEWT:8727NEWT:1182590NEWT:8726NEWT:2NEWT:157546NEWT:10090NEWT:935293NEWT:749200NEWT:35554NEWT:4120NEWT:5693NEWT:9417NEWT:347515NEWT:8724NEWT:1216979NEWT:307972NEWT:92867NEWT:8723NEWT:990346NEWT:544496NEWT:5334NEWT:145953NEWT:257309NEWT:5180NEWT:284812NEWT:115104NCBITaxon:1313NEWT:1081927NEWT:43330NEWT:67825NEWT:44544NEWT:13076NEWT:1249668NEWT:373995NEWT:544404NEWT:3702NEWT:8839NEWT:317NEWT:4232NEWT:990119NEWT:1736309NEWT:4113NEWT:7227NEWT:11298NEWT:7469NEWT:885318NEWT:171101NEWT:876138NEWT:4081NEWT:554NEWT:5691NEWT:98334NEWT:408170NEWT:260710NEWT:627025NEWT:3708NEWT:106592NEWT:237561NEWT:9913NEWT:10036NEWT:4100NEWT:7574NEWT:1351NEWT:1076NEWT:6763NEWT:7215NEWT:803NEWT:8030NEWT:380394NEWT:272563NEWT:507601NEWT:1639NEWT:188229NEWT:4909NCBITaxon:79857NEWT:95648NEWT:746360NEWT:6239NEWT:1589NEWT:135588NEWT:135622NEWT:216257NEWT:6915NEWT:9986NEWT:101510NEWT:95486NEWT:3880NEWT:58002NEWT:9103NEWT:4577NEWT:5664NEWT:2157NEWT:146479NEWT:1911079NEWT:1000589NEWT:145943NEWT:1902NEWT:85962NEWT:160488NEWT:317447NEWT:3635NEWT:7955NCBITaxon:2NEWT:1480154NEWT:7959NEWT:2261NEWT:3197NEWT:9615NEWT:884019NEWT:4565NEWT:1264690NEWT:169963NCBITaxon:38727NEWT:36329NEWT:34305NEWT:59729NCBITaxon:183674NEWT:224308NEWT:626528NEWT:139927NEWT:4558NEWT:9606NEWT:367830NEWT:157295NEWT:243230NEWT:931281NEWT:373153NEWT:7029NEWT:1283300NEWT:334747NEWT:470NCBITaxon:79824NCBITaxon:4563NEWT:3218NEWT:5759NEWT:9838NCBITaxon:9615NEWT:1736231NEWT:1193501NEWT:3055NEWT:6287NEWT:2242NEWT:6326NEWT:9796NEWT:2762NEWT:5476NEWT:1174673NEWT:562NEWT:260707NEWT:287NEWT:10117NEWT:10239NEWT:10116NEWT:1280NEWT:1836NEWT:1735272NEWT:29760NEWT:260705NEWT:80863NEWT:1148NEWT:4932NEWT:70448NEWT:9825NEWT:3603NEWT:698936NEWT:2759NEWT:39946NEWT:11676NEWT:9823NEWT:100226NCBITaxon:6073NEWT:4530NEWT:4896NEWT:6279NEWT:7370NEWT:573NEWT:6282NEWT:7091NEWT:1134506419014590000-0001-9414-9436