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"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["ltomanek@calpoly.edu"],"submitter":["Frank Fabela"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Oxidative stress","One carbon metabolism","Proteomics","Mytilus","Carbohydrate metabolism","Histone modifications","Cellular stress response"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072074"],"tissue":["Gill"],"sample_protocol":["Approximately 200 mg of gill tissue was homogenized in an 8 M urea (Thermo Scientific, Waltham, MA, USA), 2 M thiourea (Thermo Scientific, Waltham, MA, USA), and 1% deoxycholate (Spectrum Chemicals, New Brunswick, NJ, USA) denaturing buffer to improve protein solubilization while allowing for easier removal of detergents (Feist & Hummon, 2015). Cells were lysed via sonication (3 x 30 s), then kept on ice for 30 min, prior to centrifugation at 17,000 g for 30 min at 4 °C. Contaminants were removed via protein precipitation by adding 4x volume 10% trichloroacetic acid (Fisher Chemical, Pittsburg, PA, USA) in acetone (Fisher Chemical, Pittsburg, PA, USA) and storing overnight at -20 °C. Proteins were then pelleted at 17,000 g for 20 min at 4 °C, washed 2x in 1 mL 100% ice-cold acetone, and resuspended in 8 M urea with 150 mM Tris-HCl (Fisher Chemical, Pittsburg, PA, USA). Total protein concentration was determined using Pierce™ BCA Protein Assay Kit (Thermo Scientific, Waltham, MA, USA) according to manufacturer instructions. Aliquots containing 30 mg of total protein were reduced with dithiothreitol (4mM; Thermo Scientific, Waltham, MA, USA) and alkylated with iodoacetamide (18 mM; BioRad, Hercules, CA, USA). Prior to digestion in solution of Pierce™ trypsin protease (Thermo Scientific, Waltham, MA, USA), the solution was diluted to <1M urea by adding 9x volume of ammonium bicarbonate (Thermo Scientific, Waltham, MA, USA) following the manufacture protocol. Finally, peptides were desalted using Pierce™ C18 spin columns (Thermo Scientific, Waltham, MA, USA) according to manufacturer instructions and eluted to a final concentration of 750 ng/ml and analyzed using ultra-high-performance LC coupled with tandem MS (UHPLC-MS/MS) immediately following clean up. All samples were run in triplicate and 5 ml of sample was used per injection.  UHPLC-MS/MS   Peptides were separated by reverse phase chromatography (Ultimate 3000 HPLC) on a 5 mm x 300 m C18 precolumn (Thermo Scientific, Waltham, MA, USA) and then on a 150 mm x 75m (particle size 2 m) Acclaim PepMap 100 C18 LC column (Thermo Scientific, Waltham, MA, USA). We ran a linear gradient from 15% buffer B (80% acetonitrile with 0.08% formic acid (FA); Fisher Chemical, Pittsburg, PA, USA) in buffer A (0.1% FA; Fisher Chemical, Pittsburg, PA, USA), to 50% buffer B in 90 minutes at a flow rate of 300 nl·min-1. Eluted peptides were sprayed into the Q Exactive Plus Hybrid Quadrupole-Orbitrap MS (Thermo Scientific, Waltham, MA, USA) using the Nanospray Flex™ Ion Source with the following parameters: spray voltage, 2.4 kV; capillary temperature, 275°C; S-lens RF level, 50. For Data Dependent Acquisition, full MS positive ion scans were taken between 375 and 1575 m/z at a resolution of 70,000 with Automatic Gain Control (AGC) target of 3e6 at a maximum injection time of 100 ms. MS/MS scans were taken at a resolution of 17,500 with an AGC target of 1e5 with a maximum injection time of 50 ms. The top 10 precursor ions were fragmented using collision induced fragmentation at a normalized collisional energy of 27%. Dynamic exclusion was used with a duration of 20 s, the intensity threshold was set to 1.6 e5, with an isolation window of 2 m/z and lock masses turned on."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["MS Data Processing and Statistical Analysis   Data were acquired with Thermo’s Tune v.2.12 build 3134 and XCalibur v. 4.4.16.14 and peptides were analyzed using Proteome Discoverer v.2.3 (PD). The processing and consensus workflows were based upon those described in (Griss et al., 2019). MS Amanda was used as a database node for protein identification with the following parameters: a protein database from Mytilus galloprovincialis (Lamark) (NCBI taxonomy ID: 29158) was used for predicted proteins, allowing for trypsin digestion with 3 missed cleavages, an MS1 tolerance of 7 ppm, and an MS/MS tolerance of 0.03 Da. Settings searched for static carbamidomethyl modifications on cysteine, dynamic oxidation modifications on methionine, and acetyl modifications on the N-terminus of peptides (as this study also investigated the role of NAD-dependent deacetylases). Protein ID was compared to concatenated target decoy proteins. Proteins were scored based on a false discovery rate (FDR) of p<0.01 for high confidence proteins and p<0.05 for low confidence proteins. Precursor parent ion tolerance was set to 5 ppm, with a fragment tolerance of 0.02 Da at a precision of 0.999 for high confident peptides.    Label-free quantitation, including peptide data filtering, protein matching, and statistical analysis comparisons was performed in MSstats R package v.4.6.5 (Choi et al., 2017). Briefly, max peak area was used to quantify peptide abundance in PD then unique peptides were matched to proteins using an FDR of 2% in MSstats. Only unique peptides, peptides matched to only one protein, and proteins with three matched peptides were used for analysis. The most intense peak area measured per peptide were log2 transformed and median normalized by shifting intensities by a constant to make the median constant across MS runs. Run-level summarization was performed using Tukey’s median polish method, generating model estimates using peptide medians within and across technical replicates providing robustness against outliers. Model estimation within MSstats proceeded in two steps, using a linear mixed-effects model, with both biological and technical replicates included. A whole plot that includes the overall model median, plus the condition and subject by condition variation and the run variation and a subplot that includes the run variation and error term for each feature (i.e., peptide intensity) by run combination. For reasons explained in Kohler et al. (2023), the subplot can be analyzed with an ANOVA-style summarization, while the whole plot estimation is based on a restricted maximum likelihood (REML) procedure. Differential abundance (a = 0.05) was determined by comparing the response of mussels 1 h or 24 h after heat shock to the relative baseline acclimation conditions (Fig. 1C), within acclimation group.   The p-values were adjusted for multiple comparisons based on Benjamini and Hochberg (1995), which also represents the FDR. Model assumptions for normal distribution and constant variance of measurement errors can be verified visually in MSstats. Heatmaps were produced in R utilizing “pheatmap” (Kolde, 2025) and “ComplexHeatmap” (Gu et al., 2016) packages. ProBatch (Cuklina et al., 2021) was used to conduct quality control check for batch effects and peptide normality distributions."],"omics_type":["Proteomics"],"labhead":["Lars Tomanek"],"instrument_platform":[""],"labhead_affiliation":["California Polytechnic State University San Luis Obispo ;Biological Sciences Department ; California Unites States"],"submission_type":["COMPLETE"],"species":["Mytilus Californianus"],"publication":["10.1242/JEB.252105"],"submitter_mail":["fabela.frank@gmail.com"],"submitter_affiliation":["California Polytechnic State University San Luis Obispo"],"submitter_country":["United States"],"doi":["10.6019/PXD072074"],"additional_accession":[]},"is_claimable":false,"name":"Food Dependent Activation of One Carbon Metabolism During Heat Shock in Mytilus californianus","description":"Of the ecological factors affecting the cellular stress response (CSR), food ration has received little attention despite a likely role in stress tolerance limits. To test the interactive effects of food and temperature on the proteomic response to heat shock, the intertidal mussel Mytilus californianus was acclimated to four combinations of nearshore (low) and aquaculture (high) phytoplankton levels, combined with low (20 °C) and high (30 °C) aerial temperatures during daytime low tides. Whole mussels were then exposed to an acute (6 h), aerial heat stress (33 °C) and allowed to recover for 1 h and 24 h in pre-exposure conditions. Proteomic changes in the gill before and after heat shock were measured using liquid-chromatography-mass spectrometry and label-free quantification. Mussels acclimated to low-temperature-low-food (LTLF) elicited a greater heat shock response compared to other acclimation groups, increasing protein levels of core carbohydrate and sulfide metabolism. These glycolytic metabolites proposedly feed into one-carbon metabolism (e.g., folate and methionine cycles) and connecting pathways, which also increased abundance and likely contribute to purine synthesis, methylation, and transsulfuration. These mussels additionally increased levels of proteins scavenging hydrogen peroxide, chelating ferrous iron, and maintaining reduced glutathione levels. Proteins modifying chromatin (histone) structure and regulating transcription likely link the metabolic changes to chromatin modifications, specifically through SAM-dependent methyltransferases, which may contribute to repairing DNA-damage caused by oxidative stress. Overall, our results suggest a food-dependent link between metabolism and epigenetic modifications that we hypothesize may function as an autoregulatory feedback mechanism during the CSR under tidally fluctuating conditions.     SUMMARY STATEMENT    A food-dependent link between metabolism and epigenetic modifications may function as an autoregulatory feedback mechanism to repair DNA damage and scavenge oxidants during heat stress.","dates":{"publication":"2026-07-28","submission":"2025-12-17"},"accession":"PXD072074","cross_references":{"TAXONOMY":["NEWT:68239","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:37919","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2709072","NEWT:2499525","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","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:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:29466","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:2003758","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","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:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","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:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:595495","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:510516","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:1170227","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:9900","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:9979","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:352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