{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/FlagellarProteome_28_Rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/FlagellarProteome_18_Rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/Secretome_28C_Rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/FlagellarProteome_18_Rep2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/Secretome_18C_Rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/FlagellarProteome_28_Rep4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/FlagellarProteome_18_Rep4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/FlagellarProteome_28_Rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/FlagellarProteome_28_Rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/Secretome_18C_Rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/Secretome_28C_Rep1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/FlagellarProteome_18_Rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/Secretome_28C_Rep3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/Secretome_18C_Rep2.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/flagProtFiles.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD067459/SuppProtFiles.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["m.mittag@uni-jena.de"],"submitter":["PRATEEK SHETTY"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Ambient temperature","Secretome","Flagellar proteome","Chlamydomonas"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067459"],"tissue":["Cell Culture"],"sample_protocol":["For the analysis of the proteins in the MMA fraction, 0.5 mg proteins of each MMA fraction were reduced and carbamidomethylated according to Zhang et al., 2005. Samples were then subjected to the single-pot, solid phase-enhanced sample preparation (SP3) according to Hughes et al., (2019). Briefly, the proteins were bound to magnetic SP3 beads, washed three times to remove contaminants, and digested overnight at 37 °C directly on the beads by adding 20 µg of a Trypsin and LysC protease mix (MS grade, Promega V507A) dissolved in 40 µL of the provided buffer per 0.5 mg sample in Eppendorf Protein LoBind tubes that were shaken at 1,000 rpm in a Thermomixer. Prior to the mass spectrometric analyses, the resulting peptides were further purified by reversed phase chromatography using ZipTip microtips supplemented with additional Poros R2 10 μm reversed phase material (Bösger et al., 2009), dried using a Speed-Vac and stored at – 80 °C before mass spectrometry analysis. Immediately before LC-ESI-MS/MS, peptides were reconstituted in 25 µL of 5% MeCN/0.1% TFA by vortexing thrice and a 5 min cycle of ultrasonic bath sonication. The samples were then centrifuged for 5 min at 13,000 rpm and the supernatant was transferred to MS vials for LC-MS/MS measurements.  Secretome analysis was performed using cultures grown at 18 °C and 28 °C. Cells were cultivated for four days in TAP medium, as described above. Three independent biological replicates were prepared for each temperature condition. On day 4, cultures were harvested to collect cell-free supernatants. For each sample, the culture was centrifuged at 1,000 g for 10 min to remove intact cells and large particulates. The resulting supernatant was then filtered through a 0.22 µm pore-size membrane filter (Carl Roth, Germany) to ensure complete removal of any residual cells or debris.  10 mL of the supernatant from each sample were first concentrated to 250 µL using a 3 kDa MWCO Amicon centrifugal filter. Each concentrate was transferred into an Eppendorf Protein LoBind tube and adjusted to 15 µg total protein, as determined by BCA assay. The samples were finally brought to 250 µL with 1 M triethyl ammonium bicarbonate (TEAB) buffer, yielding a final concentration of 50 mM TEAB (pH ~8.5), and incubated at 60 °C for 10 min with shaking at 1,000 rpm. The subsequent steps were performed at 22 °C with shaking at 1,500 rpm. Proteins were sequentially reduced by adding 2.5 µL TCEP to a final concentration of 5 mM and incubated for 10 min, then alkylated with 5 µL iodoacetamide to a final concentration of 10 mM for 30 min and finally quenched by adding 5 µL DTT to a final concentration of 10 mM for 15 min. Next, a 1:1 mixture of hydrophobic and hydrophilic Sera-Mag carboxylate coated magnetic beads (50 mg/mL; 2 mg total; particles E3/E7; Cytiva) were prewashed three times with 100 µL water. After washing, 2.5 µL of the bead suspension was added to each sample, followed by ethanol to a final concentration of 60%. Samples were incubated for 5 min to bind proteins. Beads were bound using a magnetic rack. The supernatant was removed, and the beads were washed three times with 400 µL of 80% ethanol and once with 400 µL of MeCN. After an air-drying step, the beads were resuspended in 50 µL of 50 mM TEAB (pH ~8.5). Proteins on the beads were digested by adding 0.5 µL of recombinant LysC (0.2 µg/µL, MS grade, Promega V1671) and incubation at 37 °C for 1 h with shaking at 1,200 rpm. Subsequently, 0.4 µL of trypsin (0.5 µg/µL, MS grade, Promega VA9000) was added, and digestion continued overnight at 37 °C with shaking at 1,200 rpm. After digestion, the supernatant was collected into a new Protein LoBind tube. The beads were washed twice with 20 µL of 1% TFA, whereby each wash was incubated for 5 min at 22 °C while shaking at 1,000 rpm. The combined supernatant and wash fractions were acidified with 1 µL of 80% TFA (to pH < 3) and desalted using a 100 µL Pierce C18 Tips (Thermo Fisher 87784). Tips were equilibrated with 100 µL of 50% MeCN/0.1% TFA twice, followed by equilibration with 100 µL of 0.1% TFA twice. Samples were loaded by slowly aspirating and dispensing the solution ten times. Tips were washed twice with 100 µL of 0.1% TFA, and bound peptides were eluted three times with 75 µL of 80% MeCN/0.1% TFA. Eluates were combined, dried in a vacuum concentrator at 35 °C, and stored at –80 °C until analysis. Immediately before LC-ESI-MS/MS, peptides were reconstituted in 25 µL of 5% MeCN/0.1% TFA by vortexing thrice and a 5 min cycle of ultrasonic bath sonication. The samples were then centrifuged for 5 min at 13,000 rpm and the supernatant was transferred to MS vials for LC-MS/MS measurements."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["LC-MS/MS analysis was performed with an Ultimate3000 Nano-HPLC system (Thermo Fisher Scientific) coupled to an Orbitrap Fusion Tribrid mass spectrometer (Thermo Fisher Scientific). Samples were analyzed using an Acclaim PepMap 100 C18 trap column (0.075 × 200 mm; Thermo Fisher Scientific) and an Aurora Ultimate XT C18 UHPLC analytical emitter column (0.075 × 250 mm; Ionopticks, Collingwood, Australia) in an EASY Spray source setting with HeatSync Column Heater (Ionopticks, Collingwood, Australia). Each sample was loaded onto the trap column, washed with 0.1% TFA in water, and then transferred to the analytical column. Peptides were separated in a 152-minute run (buffer A: water with 0.1% FA, buffer B: MeCN with 0.1% FA, flowrate: 400 nL/min) with the following gradient: from 5% B to 22% B in 105 min, from 22% B to 32% B in 10 min, from 32% B to 90% B in 10 min, hold at 90% B for 10 min,  then to 5% B over 0.1 min, and hold at 5% B for 10 min. The Orbitrap Fusion Tribrid mass spectrometer was operated in a data-dependent acquisition (DDA) mode with a cycle time of 3 s. Full scan acquisition was performed in the Orbitrap at a resolution of 120,000 in the scan range of 300 – 1,500 m/z (AGC target of 50%, maximal injection time of 50 ms). Monoisotopic precursor selection as well as dynamic exclusion (exclusion duration: 60 s) was enabled. Precursors with charge states of 2 – 7 and intensities greater than 5e3 were selected for fragmentation. Isolation was performed in the quadrupole using a window of 1.6 m/z. Fragments were generated using higher-energy collisional dissociation (HCD, normalized collision energy: 30%) and detected in the Ion Trap (scan rate: rapid, mass range: normal, maximal injection time: 35 ms, AGC target: standard).All raw LC–MS/MS data were processed with FragPipe version (v22.0), incorporating MSFragger (v4.1) for peptide identification. We applied the built in LFQ MBR workflow to search against the publicly available Chlamydomonas v6.1 reference proteome database supplemented with common contaminants and decoy sequences (CreinhardtiiCC_4532_707_v6.1.protein_primaryTranscriptOnly.fa). MSFragger performed a closed search using initial precursor and fragment mass tolerances of 0.5 Da, followed by automatic mass recalibration and selection of narrower tolerances. The enzyme was set to strict trypsin, allowing up to two missed cleavages, with peptide lengths constrained to 7–50 residues and masses between 500 and 5,000 Da. Methionine oxidation (+15.9949 Da) and protein N terminal acetylation (+42.0106 Da) were set as variable modifications, while cysteine carbamidomethylation (+57.0215 Da) was fixed. Subsequently, MSBooster, Percolator, and Philosopher were employed to generate deep learning augmented scores, perform PSM rescoring, and estimate false discovery rates. Label-free quantification was then carried out with IonQuant (v1.10.27) under default settings, using a mass tolerance of 10 ppm and a retention time tolerance of 0.4 min. Both, “match between runs” and “MaxLFQ” algorithms were enabled. The “min scans” parameter was set to 3, “min isotopes” was set to 2, and “MaxLFQ min ions” was set to 2. Proteins were considered differentially regulated when they exhibited a |log2 fold change| > 0.5 and an adjusted P-value < 0.05. DeepLoc 2.1 (Odum et al., 2024) was used to predict the subcellular localization of identified secreted proteins, with the organism type set to \"Plant\" to optimize predictions for the Chlorophyte alga Chlamydomonas. DeepLoc 2.1 predicts localization up to ten subcellular compartments: nucleus, cytoplasm, extracellular/secreted, mitochondrion, cell membrane, endoplasmic reticulum, chloroplast, Golgi apparatus, lysosome/vacuole, and peroxisome. Proteins were classified as secreted if they received an \"extracellular\" prediction with a confidence score > 0.5."],"omics_type":["Proteomics"],"labhead":["Prof. Dr. Maria Mittag"],"instrument_platform":[""],"labhead_affiliation":["Friedrich Schiller University Matthias Schleiden Institute General Botany Am Planetarium 1 07743 Jena"],"submission_type":["PARTIAL"],"species":["Chlamydomonas Reinhardtii"],"submitter_mail":["prateekshettys@gmail.com"],"publication":["10.1093/PLCELL/KOAG136"],"submitter_affiliation":["Friedrich Schiller University,\nMatthias Schleiden Institute,\nGeneral Botany, JSMC postdoc"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"multi-omics studies reveal how ambient temperatures govern Chlamydomonas’ cellular responses","description":"Understanding microalgal responses to subtle temperature changes is critical, as they are primary producers that drive ecosystem productivity and food web dynamics. Even small shifts may alter algal fitness and reshape interactions with other microbes. In this study, C. reinhardtii was grown at non-stress, ambient temperatures of 18 °C and 28 °C. Proteomic analysis of isolated cilia and secreted proteins identified major changes in abundance within these sub-proteomes, particularly intraflagellar transport (IFT) complexes in cilia and mating-related proteins in the secretome that are both upregulated at higher 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