{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/Spectronaut_164_2024_PRIDE.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-9.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-8.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-16.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069186/164_2024_FM-7.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["mbergkessel001@dundee.ac.uk"],"submitter":["Megan Bergkessel"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Carbon starvation","Pseudomonas aeruginosa","Nitrogen starvation","Label-free quantification"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069186"],"sample_protocol":["5 ml aliquots of culture at an optical density (600 nm) of 0.2 were pelleted by centrifugation, flash frozen with liquid nitrogen and stored at -70 ̊C. The media conditions were as follows: MOPS minmal media (50mM MOPS, 40 mM NaCl, 4mM K2HPO4, 2.0 mM KCl, 1.0 mM MgSO4, 0.1 mM CaCl2, , 7.5 μM FeCl2·4H2O, 0.8 μM CoCl2·6H2O, 0.5 μM MnCl2·4H2O, 0.5 μM ZnCl2, 0.2 μM Na2MoO4·2H2O, 0.1 μM NiCl2·6H2O, 0.1 μM H3BO3, 0.01 μM CuSO4·5H2O) was supplemented with 45 mM sodium succinate for the nitrogen starvation condition, 30 mM ammonium chloride for the carbon starvation condition, or both for the nutrient replete condition. The nitrogen starvation timepoint was taken after 48 hours in nitrogen starvation media, the transition timepoint was taken immediately after switching cells to carbon starvation media, the carbon starvation timepoint was taken after a further 24 hours in carbon starvation media, and the nutrient replete timepoint was taken 7 hours after shifting cells to nutrient replete media. Cell pellets were lysed in 2% SDS, 100 mM Tris pH 8.0, 0.2 μL/mL benzonase with cOmplete EDTA-free protease inhibitor (Sigma Aldrich), clarified by spinning at high speed in a benchtop centrifuge (13,000 g for 10 minutes) and normalised to a protein concentration of 150 μg/mL using lysis buffer. Trypsin digest and suspension trapping using S-Trap Micro columns (Profiti) were performed by the University of Dundee Fingerprints Proteomics facility. Briefly, proteins were reduced (20 mM DTT for 10 minutes at 95°C) and alkylated (40 mM iodoacetamide for 30 minutes in the dark) before acidifying with phosphoric acid and loading onto S-Trap columns. After washing extensively, proteins were digested on column overnight at 37°C with 0.75µg of trypsin per sample. A second digest was repeated for 6 hours the following day. Peptides were eluted with TEAB, then 0.2% formic acid, then 0.2% formic acid plus 50% acetonitrile, then dried and resuspended in 1% formic acid. Peptides were run on a Q-Exactive HF instrument (Thermo Scientific) coupled to a Dionex Ultimate 3000 HPLC system (Thermo Scientific) with LC buffers compromising of buffer A (0.1% FA) and buffer B (80% ACN, 0.1% FA). The buffers were used to create a gradient lasting 185 minutes where the peptides were eluted from a 110cm uPAC Neo C18 column (Thermo Scientific) at a flow rate of 300nl/min. Raw data was acquired in positive and Data Independent Acquisition (DIA) mode. A scan cycle compromised a full MS scan with an m/z range of 345-1155, resolution of 60,000, Automatic Gain Control (AGC) target 3x106 and a maximum injection time of 200ms. MS scans were followed by DIA scans of dynamic window widths. DIA spectra were recorded with a first fixed mass of 200m/z, resolution of 30,000, AGC target 3x106 and a maximum IT of 55ms. Normalised collision energy was set to 25 % with a default charge state set at 3. Data for both MS scan and MS/MS DIA scan events were acquired in profile mode."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Thermo RAW files were analysed using Spectronaut version 17 (Biognosys) using directDIA. Samples were searched against the UCBPP-PA14 proteome (Uniprot reference UP000000653) with variable modifications of Oxidation(M), Dioxidation(MW), Acetyl (Protein N-term), Deamidation (NQ) and Gln->Pyro-Glu set and a fixed modification of Carbamidomethyl (C). For identification a precursor PEP (Posterior Error Probability) cutoff of 10% and a protein PEP cutoff of 7.5% were set and a false discovery rate of 1% was used. Quantification was done using the protein LFQ method Quant 2.0 (SN standard) within Spectronaut. For each sample, individual protein LFQ intensities were summed and each protein intensity divided by this sum (in millions) to convert to parts per million and normalise for differences between samples in processing and loading. The resulting values were considered reflective of the fraction of the total proteome represented by each protein, with non-detected proteins having an abundance set to 0."],"omics_type":["Proteomics"],"labhead":["Megan Bergkessel"],"instrument_platform":[""],"labhead_affiliation":["University of Dundee, School of Life Sciences, Molecular Microbiology Division"],"submission_type":["PARTIAL"],"species":["Pseudomonas Aeruginosa (strain Ucbpp-pa14)","Bacteria"],"submitter_mail":["mbergkessel001@dundee.ac.uk"],"publication":["10.1128/MSYSTEMS.01439-25"],"submitter_affiliation":["University of Dundee, School of Life Sciences, Molecular Microbiology Division"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"Total proteomes of starved Pseudomonas aeruginosa","description":"We have characterized the responses of the opportunistic pathogen Pseudomonas aeruginosa to prolonged starvation for carbon or nitrogen sources, and to transitions between these states. We find that most cells survive both types of starvation for more than a week and maintain low but robustly detectable levels of protein synthesis in the absence of growth. Nitrogen-starved cells are larger, make more proteins and retain fewer ribosomes than carbon-starved cells, indicating that distinct physiological strategies are adopted during the two starvation types. We found that the total proteomes collected from starved cells at different times during a starvation transition were not very different from each other but were distinct from those of growing cells.  By combining this dataset with a nascent (BONCAT) proteomics dataset and a transposon insertion sequencing (TnSeq) dataset, we highlight proteases and chaperones; flagellar motility; and the nitrogen-related phosphotransferase system as key fitness-impacting functions that are actively maintained by growth arrested Pseudomonas 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