{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/re221130.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/re221130.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_09.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_18.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_16.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_17.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/221130_19.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD064843/re221130.mzid"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["matt.hutchings@jic.ac.uk"],"submitter":["Gerhard Saalbach"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Orra","Streptomyces","Wbla","Venezuelae"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD064843"],"tissue":["Cell Culture"],"sample_protocol":["Selected S. venezuelae strains were lawned from single colonies onto MYM+TE (pH 7.3) agar plates with sterile cellophanes and incubated to desired time points. The lawns were scraped into 50 mL falcon tube containing 10 mL cell lysis buffer (2 % SDS, 50 mM TEAB Buffer pH 8.0, 150 mM NaCl, EDTA-free protease inhibitor tablets [Roche]). Samples were vortex vigorously to disrupt the mycelial mass and minimize clumping, then boiled for 10 minutes. Following boiling, samples were then sonicated using four 20 second pulses at 10 microns, with 1-minute intervals between each cycle. Debris was removed by centrifugation at 4,000 x g for 30 min at room temperature. The clarified supernatant was transferred to a fresh tube, and protein concentration measured using the Qubit Protein Assay. A total of 1 mg (or a minimum of 200-300 mg) total protein was aliquoted to a 15 mL Falcon tube. The remaining lysate was flash-frozen and stored as backup. Proteins were precipitated with chloroform/methanol. Protein pellets were resuspended in 100 µl of 2.5% sodium deoxycholate (SDC; Merck) in 0.2 M EPPS-buffer (Merck), pH 8.5, and vortexed and heated to ~90°C for a total of three cycles. Protein concentration was estimated using a BCA assay and approx. 200 µg of protein per sample was reduced, alkylated, and digested with trypsin in the SDC buffer according to standard procedures. After the digest, the SDC was precipitated by adjusting to 0.2% trifluoroacetic acid (TFA), and the clear supernatant subjected to C18 SPE. TMT labelling was performed using 6 channels from a TMT™16plex kit (Lot WJ329096, ThermoFisher Scientific) according to the manufacturer’s instructions with slight modifications; approx. 100 µg of the dried peptides were dissolved in 90 µl of 0.2 M EPPS buffer (Merck)/10% acetonitrile, and 250 µg TMT reagent dissolved in 22 µl of acetonitrile was added. After 2 h incubation, aliquots of 2 µl from each sample were combined in 400 µl 0.2% TFA, desalted, and analysed on the mass spectrometer to check labelling efficiency and estimate total sample abundances. The main sample aliquots were then quenched with 8 µl of 5% hydroxylamine and combined correspondingly to roughly level abundances. The combined samples were desalted using a C18 Sep-Pak cartridge (200 mg, Waters), redissolved in 500 µl of 25 mM NH4HCO3 and fractionated by high pH reversed phase HPLC. Using an ACQUITY Arc Bio System (Waters), the samples were loaded to an XBridge® 5 µm BEH C18 130 Å column (250 x 4.6 mm, Waters). Fractionation was performed with the following gradient of solvents A (water), B (acetonitrile), and C (25 mM NH4HCO3  in water) at a flow rate of 1 ml min-1: solvent C was kept at 10% throughout the gradient; solvent B: 0-5 min: 5%, 5-10 min: 5-10%, 10-80 min: 10-45%, 80-90 min: 45-80%, followed by 5 min at 80% B and re-equilibration to 5% for 24 min. Fractions of 1 ml were collected and concatenated to produce 19 fractions for MS analysis. Aliquots were analysed by nanoLC-MS/MS on an Orbitrap Eclipse™ Tribrid™ mass spectrometer equipped with a FAIMS Pro Duo interface coupled to an UltiMate® 3000 RSLCnano LC system (Thermo Fisher Scientific, Hemel Hempstead, UK). The samples were loaded onto a trap cartridge (Pepmap 100, C18, 5um, 0.3x5mm, Thermo) with 0.1% TFA at 15 µl min-1 for 3 min. The trap column was then switched in-line with the analytical column, a nanoEase M/Z column (HSS C18 T3, 1.8 µm, 100 Å, 250 mm x 0.75 µm, Waters). The following gradient of solvents A (water, 0.1% formic acid) and B (80% acetonitrile, 0.1% formic acid) was used at 40°C at a flow rate of 0.2 µl min-1 : 0-3 min 3% B (parallel to trapping); 3-10 min linear increase B to 8 % (curve 4); 10-108 min linear increase B to 50%;  108-113 min linear increase B to 99 %; kept at 99% B for 3 min and re-equilibration to 3% B. Data were acquired on the mass spectrometer with the following parameters in positive ion mode: MS1/OT: resolution 120K, profile mode, mass range m/z 400-1600, AGC target 4e5, max inject time 50 ms, FAIMS device set to three compensation voltages (-35V, -50V, -65V) for 1 s each; MS2/IT: for each CV, data dependent analysis with the following parameters: 1 s cycle time Rapid mode, centroid mode, quadrupole isolation window 0.7 Da, charge states 2-5, threshold 1.9e4, CID CE = 30, AGC target 1e4, max. inject time 50 ms, dynamic exclusion 1 count for 15 s  mass tolerance of 7 ppm; MS3 synchronous precursor selection (SPS): 10 SPS precursors, isolation window 0.7 Da, HCD fragmentation with CE=50, Orbitrap Turbo TMT and TMTpro resolution 30k, AGC target 1e5, max inject time 100 ms, Real Time Search (RTS): protein database Streptomyces venezuelae (7420 entries, from Streptomyces venezuelae strain NRRL B-65442 chromosome - Nucleotide - NCBI (nih.gov)), enzyme trypsin, 1 missed cleavage, oxidation (M) as variable, carbamidomethyl (C) and TMTpro as fixed modifications, precursor tolerance 10 ppm, Xcorr = 1.4, dCn = 0.1."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The mass spectrometry raw data were processed and quantified in Proteome Discoverer 3.2 (Thermo Fisher Scientific); all mentioned tools of the following workflow are nodes of the proprietary Proteome Discoverer (PD) software.   The S. venezuelae fasta database (as above for RTS) was imported into PD adding a reversed sequence database for decoy searches; a database for common contaminants (maxquant.org, 245 entries) was also included. The database search was performed using the incorporated search engines CHIMERYS (MSAID, Munich, Germany) and Comet [REF]. The processing workflow included recalibration (RC) of MS1 spectra, reporter ion quantification by most confident centroid (20 ppm) and a search on the imported S. venezuelae database. The Top N Peak Filter was applied with 20 peaks per 100 Da. For CHIMERYS, the inferys_4.7.0._fragmentation prediction model was used with fragment tolerance of 0.3 Da, enzyme trypsin with 1 missed cleavage, variable modification oxidation (M), fixed modifications carbamidomethyl (C) and TMTpro on N-terminus and K. For Comet the version 2019.01 rev.0 parameter file was used with default settings except precursor tolerance set to 6 ppm and trypsin missed cleavages set to 1. Modifications were the same as for CHIMERYS. The consensus workflow included the following parameters: intensity-based abundance, normalisation on total peptide abundances, protein abundance-based ratio calculation, only unique peptides (protein groups) for quantification, TMT channel correction values applied (according to the TMT kit lots mentioned above), co-isolation/SPS matches/CHIMERYS Coefficient thresholds 50%/65%, 0.8, missing values imputation by low abundance resampling, hypothesis testing by t-test (background based), adjusted p-value calculation by BH-method. The results were exported into a Microsoft Excel table including data for normalised and un-normalised abundances, ratios for the specified conditions, the corresponding p-values and adjusted p-values, number of unique peptides, q-values, PEP-values,  identification scores from both search engines; FDR confidence filtered for high confidence (strict FDR 0.01) only."],"omics_type":["Proteomics"],"labhead":["Matt Hutchings"],"instrument_platform":[""],"labhead_affiliation":["John Innes Centre Dept. Molecular Microbiology Norwich Research Park Norwich, UK"],"submission_type":["COMPLETE"],"species":["Streptomyces Venezuelae"],"submitter_mail":["gerhard.saalbach@jic.ac.uk"],"publication":["10.1099/MIC.0.001706"],"submitter_affiliation":["Biological Chemistry"],"submitter_country":["United Kingdom"],"doi":["10.6019/PXD064843"],"additional_accession":[]},"is_claimable":false,"name":"Identification of a regulatory cascade that activates chloramphenicol biosynthesis in Streptomyces venezuelae","description":"Specialised metabolites made by the genus Streptomyces form the basis of 55% of clinically used antibiotics as well as cancer therapeutics, immunosuppressants and other anti-infectives. Streptomyces venezuelae is a model for the genus because it is fast-growing, sporulates in liquid culture within 24 hours and coordinates production of the antibiotic chloramphenicol with sporulation. In this work we demonstrate that chloramphenicol biosynthesis is controlled by a regulatory cascade involving the developmental transcription factors OrrA, WblA and AdpA. OrrA directly activates the production of the WhiB-family protein WblA which binds to 90 target gene promoters, including adpA. AdpA is a pleiotropic regulator that directly activates chloramphenicol biosynthesis, and we propose that deletion of orrA or wblA results in an increase in the levels of AdpA which in turn leads to the increase in chloramphenicol biosynthesis observed in these 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