{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD061965/Q25070-23-120-iodoTMT.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD061965/PRIDE_Sample_List.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD061965/Q25070-23-120-07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD061965/Q25070-23-120-06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD061965/Q25070-23-120-08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD061965/Q25070-23-120-10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD061965/Q25070-23-120-09.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["m.luzarowski@zmbh.uni-heidelberg.de"],"submitter":["Marcin Luzarowski"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Presequence processing","Reactive oxygen species","Mitochondrial protein biogenesis","Mitochondrial unfolded protein response"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD061965"],"sample_protocol":["Protein precipitation was performed using a chloroform/methanol method (Wessel and Flügge, 1984). Briefly, 50 μl of each sample was mixed with 50 μl lysis buffer (6 M urea, 200 mM Tris-HCl pH 8.5, 5 mM EDTA, 0.5% SDS) and incubated for 5 min at room temperature. The mixture was combined with 400 μl methanol, vortexed, and centrifuged at 9000 × g for 10 s. Following the addition of 100 μl chloroform, the samples were vortexed and centrifuged again. Phase separation was induced by adding 300 μl water, followed by centrifugation at 9000 × g for 1 min. The upper aqueous phase was discarded, and proteins were pelleted by adding 300 μl methanol, vortexing, and centrifugation at 9000 × g for 2 min. The supernatant was removed, and the pellet was air-dried before resuspension in 80 μl urea buffer (6 M urea, 200 mM Tris-HCl pH 8.5, 5 mM EDTA). The protein solution was vortexed, incubated on a shaker for 10 min, sonicated for 10 min, and incubated again on a shaker for 10 min. Protein concentration was determined using the Bradford assay (Bio-Rad Protein Assay #5000006) (Bradford, 1976). Each sample was divided into two equal aliquots: one for quantification of oxidized cysteines and the other for total protein analysis. The final protein amount was adjusted to 100 μg per sample in 50 μl urea buffer. The following protocol is based on the previously published work (Shakir et al., 2017). For alkylation of reduced thiols, 50 μl of 400 mM iodoacetamide (IAM) in urea buffer was added to half of the samples, resulting in a final IAM concentration of 200 mM. The mixture was incubated at 37°C for 1 h in the dark with continuous shaking at 1300 rpm. The reaction was quenched by adding 400 μl of −20°C acetone, vortexing, and storing the samples at −20°C overnight. The following day, protein pellets were collected by centrifugation at 13,000 × g for 30 min at 4°C, washed once with cold acetone and twice with acetonitrile, and air-dried. The pellets were resuspended in 50 μl urea buffer and subjected to sonication and incubation to ensure complete solubilization. The remaining samples, not treated with IAM in the first step were adjusted to 50 μl with urea buffer. For the reduction of disulfide bonds, 50 μl of 40 mM dithiothreitol (DTT) in urea buffer was added to all samples, yielding a final concentration of 20 mM DTT. Samples were incubated at 37°C for 2 h with shaking. Proteins were precipitated by adding 400 μl −20°C acetone, vortexing, and storing at −20°C overnight. The next day, pellets were processed as described above. For iodoTMT labeling, protein pellets were resuspended in 100 μl urea buffer. 20 μl of the sample was used to prepare a reference sample, used for data normalization. The reference sample is a mixture of all four sample types. The remaining 80 μl was subjected to iodoTMT labeling. The iodoTMT reagent was reconstituted in 20 μl methanol, vortexed, and mixed with the protein sample. After brief centrifugation, the reaction was incubated at 37°C for 2 h in the dark with shaking. Proteins were precipitated by adding 400 μl −20°C acetone, vortexing, and storing at −20°C overnight. The next day, labeled proteins were pelleted, washed, and air-dried as described above. Protein pellets were dissolved in 40 μl digestion buffer (8 M urea, 100 mM NaCl, 50 mM triethylammonium bicarbonate [TEAB] pH 8.5), incubated on a shaker for 10 min, sonicated for 10 min, and incubated again for 10 min. The pH was confirmed to be ~8.5. Proteins were digested sequentially with Lys-C and trypsin. First, Lys-C was added at a 1:100 enzyme-to-protein ratio, and samples were incubated at 37°C for 4 h. The urea concentration was then reduced to 1.6 M by dilution with 50 mM Tris-HCl pH 8.5. Trypsin was added at a 1:50 to 1:100 enzyme-to-protein ratio, and digestion proceeded overnight at 37°C. The reaction was stopped by adjusting the pH to <2 with trifluoroacetic acid (TFA, final concentration 0.4% v/v). After centrifugation at 2500 × g for 10 min, the peptide-containing supernatant was transferred to a fresh microtube. Peptides were desalted using SepPak C18 solid-phase extraction (SPE) cartridges (Waters, WAT036820). Cartridges were conditioned with 100% acetonitrile (ACN) followed by 50% ACN/0.1% TFA. Equilibration was performed using 0.1% TFA. Acidified peptide samples were loaded dropwise, and the flow-through was collected. The column was washed with 0.1% TFA before elution with 80% ACN containing 0.1% TFA. Eluted peptides were dried using a centrifugal evaporator and stored at −20°C until further analysis."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Samples were suspended in 0.1% TFA and analyzed using an Ultimate 3000 liquid chromatography system coupled to an Orbitrap QE HF (Thermo Fisher) as described before (Pedre et al. 2023). Briefly, peptides were separated in a 120 min linear gradient optimized for TMT-labeled peptides, starting from 3% B and increasing to 28% B over 100 min and to 44% B over 20 min, followed by washout with 95% B. Mass spectrometry analysis was performed using an Orbitrap mass spectrometer in data-dependent acquisition mode, switching automatically between MS and MS2 scans. Full MS spectra were acquired in the Orbitrap mass analyzer over an m/z range of 400–1600 at a resolution of 60,000 (m/z 400). The automatic gain control (AGC) target was set to 1 × 106, with a maximum injection time (IT) of 100 ms. For MS2 scans, up to 15 precursors were selected for fragmentation using higher-energy collisional dissociation (HCD) with a normalized collision energy (NCE) of 32 and an isolation width of 0.7 m/z. Fragment ions were detected in the Orbitrap at a resolution of 30,000, with an AGC target of 1 × 105 and a maximum IT of 50 ms. Precursors with charge states of 1, 6-8, and >8 were excluded from selection. Dynamic exclusion was enabled with a 20 s exclusion duration. The first fixed mass for MS2 scans was set to 100.0 m/z. MS/MS spectra were searched against the Swiss-Prot S. cerevisiae (UP000002311) database and a customized contaminant database using Proteome Discoverer 2.5 (Thermo Fisher Scientific) with the Sequest HT search algorithm (Eng et al., 1994). Trypsin was specified as the proteolytic enzyme, allowing up to two missed cleavages. The precursor ion mass tolerance was set to 10 ppm, and the fragment ion mass tolerance was set to 0.02 Da. Dynamic modifications included oxidation of methionine, carbamidomethylation of cysteine, iodoTMT modification of cysteine (+329.277 Da), and acetylation of the protein N-terminus. Peptide quantification was performed using the reporter ion quantifier node, with reporter abundance calculated based on intensity, and a co-isolation threshold set to 50%. The false discovery rate (FDR) for peptide and protein identification was controlled at <1% using the Percolator algorithm. All data analyses were performed using R within the RStudio environment . Peptide group data were imported into R for further processing. Only peptides with an Xcorr score ≥1, identified as S. cerevisiae-derived, and carrying an iodoTMT modification were considered for downstream analysis. To focus on mitochondrial proteins, the dataset was filtered to retain only proteins annotated with mitochondrial localization. To account for potential technical variability, peptide intensities were normalized within experimental groups using a median-centering approach, ensuring comparable intensity distributions across conditions. Peptides were further filtered to retain only those quantified in at least three biological replicates in at least one experimental group. Missing values were imputed using the missForest algorithm from the R package missForest, which employs a random forest-based approach for robust imputation . Peptide intensities were then scaled relative to reference samples included in each multiplexed analysis. The relative oxidation levels of cysteine-containing peptides were determined by calculating the ratio of oxidized cysteine peptides to the total abundance of cysteine-containing peptides for both control and D-Ala-treated conditions. The statistical significance of differential oxidation levels was assessed using two-tailed Student’s t-tests. The resulting p-values were adjusted for multiple testing using the Benjamini-Hochberg method to control the false discovery rate (FDR)."],"omics_type":["Proteomics"],"labhead":["Marcin Luzarowski"],"instrument_platform":[""],"labhead_affiliation":["Core Facility for Mass Spectrometry and Proteomics, Center for Molecular Biology of Heidelberg University (ZMBH), DKFZ-ZMBH Alliance, 69120 Heidelberg, Germany"],"submission_type":["PARTIAL"],"species":["Saccharomyces Cerevisiae (baker's Yeast)"],"publication":["Not available"],"submitter_mail":["m.luzarowski@zmbh.uni-heidelberg.de"],"submitter_affiliation":["University of Heidelberg"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Mitochondrial surveillance activates the primary UPRmt","description":"The mitochondrial unfolded protein response (UPRmt) is critical for protecting mitochondria against proteotoxic stress. Current UPRmt models propose that mitochondrial defects are detected by cytosolic surveillance mechanisms after release of damage into the cytosol. However, these findings are based on models that induce rapid and severe mitochondrial dysfunction, and thus their mode of toxicity contrasts sharply from physiologically occurring mitochondrial damage, e.g. the gradual accumulation of reactive oxygen species (ROS) during age-related decline or chronic respiratory chain defects. Here, we employed a chemogenetic strategy that induces low levels of H2O2 in the mitochondrial matrix to investigate cellular responses to physiologically relevant levels of mitochondrial dysfunction. We uncover that this mild oxidative stress activates the UPRmt independently of cytosolic signals revealing a so far concealed primary surveillance mechanism within mitochondria. Moreover, we identify the mitochondrial presequence proteases MPP and Oct1 as early molecular targets of ROS: Oxidative stress induces glutathionylation of critical cysteine residues, resulting in diminished proteolytic activity and the accumulation of proteotoxic precursor aggregates in the matrix. These aggregates are detected by intramitochondrial surveillance systems, activating UPRmt signaling. Our findings uncover the primary response to mitochondrial dysfunction, and highlight the organelle's capacity for self-surveillance and its ability to initiate early and rapid protective signaling in the face of mitochondrial dysfunction.","dates":{"publication":"2026-04-07","submission":"2025-03-18"},"accession":"PXD061965","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:2042545","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:109376","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:5535","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:305400","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:32224","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:393133","NEWT:65125","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: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:292415","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:367737","NEWT:936350","NEWT:1883446","NEWT:380703","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:175694","NEWT:1883456","NEWT:1195466","NEWT:2483192","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:1002697","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:51351","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:630390","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:10835","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:353154","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NE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