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Aranguren-Gassis"],"technology_type":["mass spectrometry imaging","Mass Spectrometry"],"software":["Not available"],"submitter_keywords":["Temperature","Lc-ms/ms","Marine diatom"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057782"],"tissue":["Cell Culture"],"sample_protocol":["Experiments: four populations of Chaetoceros simplex Ostenfeld (strain CCMP 200 from the National Center for Marine Algae and Microbiota, NCMA) were cultured during ~200 generations under above-optimum temperature (31ºC), and one population was maintained at 25ºC as a control. The details of the evolution experiment are described in Aranguren-Gassis et al. (2019).  Two evolved populations were randomly selected from the ones that developed high-temperature (34ºC) tolerance (thermo-tolerant, Tt populations), and other two populations were randomly selected from the control replicates (nontolerant, Nt populations), one maintained at 25ºC and one from the cryopreserved ancestral populations. Those populations were grown at the ancestral optimum temperature (25ºC) and at the above-optimal temperatures (31ºC for the Nt and 34ºC for the Tt).  After at least 2 days of acclimation, and while cultures were growing exponentially, 100 ml of each culture were filtered onto 0.2 um pore size polycarbonate membrane filters with gentle vacuum pressure. The filters were immediately frozen in liquid nitrogen and preserved at -80ºC until protein extraction.  Proteins extraction The equipment was washed before extraction, first with methanol, then with ethanol 70%, and finally with 100% ethanol. All reactants were prepared with HPLC grade water, and the tubes used for processing samples were low binding types. Frozen filters were washed with 0.5 M Tetraethylammonium bicarbonate (TEAB) buffer solution with 0.1% sodium dodecyl sulfate (SDS) detergent. The filtered biomass was ground in a precooled mortar with liquid nitrogen and 1ml 1% protease inhibitor solution (Thermo Fisher protease and phosphatase inhibition cocktail without EDTA). The ground samples were sonicated for 5 minutes with ice, and then 100 μl glass beads (Sigma acid washed glass beads 425-600 µm) were added to each sample. They were bead beaten 5 times, alternating 2 minutes beating and 2 minutes resting in ice.  After beating, samples were centrifugated at 4ºC  and 18000g for 30 minutes. The supernatant was then transferred to new tubes and stored at -80ºC.   Proteomic analyses 1-Quantification Bicinchoninic acid (BCA) microplate assay (Thermo Scientific Pierce BCA Protein Assay Kit) was used for protein quantification with an albumin (Sigma Aldrich bovine serum albumin) calibration standard. For each sample, 15 μg protein was diluted in acetone to obtain 1 μg/μl protein concentration and stored at -20ºC for 12 hours. Samples were then centrifugated (4ºC 10000 g 10 minutes), and the pellets were resuspended in 15 μl of TEAB 20 mM solution.   2- In-gel digestion of proteins Protein samples containing 10 µg of total protein were loaded onto a standard Laemmli-type polyacrylamide gel and allowed to stack and enter the resolving gel, but not allowed to separate. Comassie blue stain was used. Then, gel pieces were excised and subjected to in-gel digestion. Briefly, gel pieces were washed sequentially with ammonium bicarbonate 25 mM and 50% ACN/ammonium bicarbonate 25 mM, in an ultrasonic bath; proteins were reduced by treatment with 10mM DTT for 1 hour, and alkylated with 55mM IAA for 30 min. Protein digestion was accomplished with 40 ng of trypsin at 37 ºC overnight and tryptic peptides were extracted from the gel matrix in two steps with 0,5% TFA and 100% ACN. 3- LC-MS/MS analysis The tryptic peptides were dried in a speed-vacuum concentrator at 45ºC (Concentrator plus, Eppendorf, Hamburg, Germany), reconstituted in LC/MS-grade water containing 0.1% (v/v) formic acid and analysed by electrospray ionization-tandem mass spectrometry on a hybrid high-resolution LTQ-Orbitrap Elite mass spectrometer coupled to a Proxeon Easy-nLC 1000 UHPLC system (ThermoFisher Scientific).  The peptides were delivered onto a reverse phase column (PepMap® RSLC C18, 2µm, 100 Å, 75µm x 50cm, Thermo Fisher Scientific) and were eluted with an ACN gradient of 5-30% containing 0.1% formic acid for 240 min. The elutes were directly delivered into the mass spectrometer, which was set in positive ion mode in a data-dependent manner. A full MS scan was performed from 380−1600 m/z with resolution at 120,000. The tandem mass spectrometer (MS/MS) CID (Collision-Induced Dissociation was performed with top 15 at 38% of the normalized collision energy (NCE) with a dynamic exclusion time at 30 s, a minimum signal threshold at 1000, a resolution at 30,000, and an isolation width at 1.50 Da."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Transcriptomics Transcripts were assembled using the RNAseq Annotation Pipeline (RAP). The raw paired-end Illumina fastq files were trimmed of any existing primers and the low quality bases (primer-trim & qtrim) and filtered for rRNA sequences. The preprocessed (filtered) sequences were initially used for assembling the contigs at library level. The resulting contigs were then merged by groups. Open reading frames (ORFs) were identified for the merged assembled contigs. Read counts for each ORF were tabulated by mapping the original reads to the assembled contigs of each group. Functional annotation of each ORF was generated using BLAST, HMMER, TMHMM, transporter, organelle & KOG searches of the curated reference sequences in phyloDB database. Protein identification and quantification PEAKS Studio v.8.0 software (Bioinformatics Solutions Inc., Waterloo, Canada) was used for matching MS/MS spectra against the database (open reading frames from RNAseq) obtained from the transcriptomic analyses described above. Prior to identification, a data refinement was made with default predefined parameters.  PEAKS DB tool was used for the proteins identification against Ch. simplex transcriptomics results.  10 ppm and 0.02 Da were set for precursor and fragment ion tolerance respectively; up to one missed trypsin cleavage site allowed. Oxidation of methionine and N-terminal acetylation were set as variable modifications, while carbamidomethylation of cysteine residues was set as fixed modifications. False Discovery Rate (FDR) was set at 0.1% at PSM level.  For Label Free quantification, peptide intensities for each sample were normalized based on the total ion chromatogram (TIC). Only identifications of unique peptides were used for protein quantification. Parameter settings were: Mass Error Tolerance: 10.0 ppm; Retention Time Shift Tolerance: 5.0 min; Dependent on PID: 46; FDR Threshold: 1%. From the identified proteins, only those present in at least 50% of the replicates for each treatment were considered for the subsequent analyses."],"omics_type":["Proteomics"],"labhead":["Emilio Fernández"],"instrument_platform":[""],"labhead_affiliation":["University of Vigo"],"submission_type":["COMPLETE"],"species":["Chaetoceros Simplex"],"publication":["10.1111/1462-2920.70341"],"submitter_mail":["aranguren@uvigo.gal"],"submitter_affiliation":["University of Vigo"],"submitter_country":["Spain"],"doi":["10.6019/PXD057782"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic response of marine diatoms to thermal stress","description":"In this study, we present the proteomic response of Chaetoceros simplex, a marine diatom, to varying temperatures. We aim to explore the differing responses to thermal stress between a thermo-tolerant strain and a non-thermo-tolerant strain.","dates":{"publication":"2026-06-03","submission":"2024-11-12"},"accession":"PXD057782","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:48106","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT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