{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/3608rd_23final_250830_.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_20.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_23.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_21.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_19.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_18.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_22.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_17.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_09.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_16.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069151/250905_.mzid"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["Matt.Hutchings@jic.ac.uk"],"submitter":["Gerhard Saalbach"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Mtra","Sporulation","Streptomyces","Whii","Response regulators","Bldm"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069151"],"tissue":["Cell Culture"],"sample_protocol":["S. venezuelae colonies were grown on cellophane covered MYM or R2YE agar plates as triplicate spots from 5 µl spores, all in duplicate. After 5 days at 30 °C the mycelium was scraped into a 15 ml Falcon tube and resuspended in 10 ml cell lysis buffer [50 mM TEAB buffer pH 8.0, 150 mM NaCl, 2% SDS, EDTA-free protease inhibitor, PhosSTOP phosphatase inhibitor (Sigma Aldrich)]. The suspension was disrupted via French press three times before being boiled for 10 min. Samples were sonicated at 50 kHz four times for 20 s per cycle and then pelleted at 4000 r.p.m. for 30 min. Protein concentration was determined using the BCA assay and 1 mg of protein from each sample transferred to a fresh 15 ml Falcon tube. Samples were processed and analysed as described previously (30). The protein pellets were resuspended in 250 µl of 2.5% sodium deoxycholate (SDC; Merck) in 0.2 M EPPS-buffer (Merck), pH 8.5, and vortexed under heating. Protein concentration was estimated using a BCA assay. For the analysis, approx. 100 µg of protein per sample was used. The proteins were treated with DTT (10 mM, 60°C, 45 min) and iodoacetamide (30 mM, 45 min) to reduce and alkylate cysteine residues. One µg of Trypsin (Sequencing Grade, Promega) was added per sample and the samples were incubated at 40°C for about 18 h. After the digest, TMT labelling was performed using 12 channels from a TMT™16plex kit (Lot ZD386952, ThermoFisher Scientific) according to the manufacturer’s instructions. Samples were assigned to the TMT channels in alternating order to avoid channel leakage according to [REF_1] between different conditions with channels 126, 130N, 130C, 131N omitted.  After 2 h incubation, aliquots of 2 µl from each sample were combined in 600 µl 0.5% TFA, desalted, and analysed on the mass spectrometer (same method as for TMT, but without RTS, see below) to test labelling efficiency and estimate total sample abundances. The main sample aliquots were quenched by adding 8 µl of 5% hydroxylamine and then combined to roughly level abundances according to the test and desalted using a C18 Sep-Pak cartridge (200 mg, Waters). The eluted peptides were dissolved 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, pH 8.5) 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 25 min. Fractions of 1 ml were collected and concatenated by combining distant fractions of similar peptide concentration to produce 23 final 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 and coupled to a Vanquish™ Neo UHPLC System (Thermo Fisher Scientific, Hemel Hempstead, UK). The samples were loaded onto a trap cartridge (PepMap™ Neo Trap Cartridge, C18, 5um, 0.3x5mm, Thermo) with 10 µl of 0.1% TFA at 15 µl min-1. The trap column was then switched in-line with the analytical column (Aurora Frontier TS, 60 cm nanoflow UHPLC column, ID 75 µm, reversed phase C18, 1.7 µm, 120 Å; IonOpticks, Fitzroy, Australia) for separation at 60°C using the following gradient of solvents A (water, 0.1% formic acid) and B (80% acetonitrile, 0.1% formic acid) at a flow rate of 0.25 µl min-1:  0-7 min increase B from 1% to 7% (curve 4), 7-107 min  increase B to 46% (or 52% depending on fraction); 107-112 min linear increase B to 99 %; keeping at 99% B for 3 min and re-equilibration to 1% B. Data were acquired 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 30 s, mass tolerance ± 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 200%, max inject time 100 ms, Real Time Search (RTS): protein database Streptomyces venezuelae (7420 entries), enzyme trypsin, 1 missed cleavage, oxidation (M) as variable, carbamidomethyl (C) and TMTpro as fixed modifications, precursor tolerance 10 ppm, match parameters: 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); all mentioned tools of the following workflow are nodes of the proprietary Proteome Discoverer (PD) software. The S. venezuelae database (7420 entries) 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_2]. 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 TopN 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 5 ppm and trypsin missed cleavages set to 1. Modifications were the same as for CHIMERYS. The consensus workflow included the following parameters: use of 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 (Lot ZD386952), 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 the Benjamini-Hochberg procedure. The results were filtered for strict FDR confidence (0.01) and Master proteins and were exported into a Microsoft Excel table including, among others, results for normalised and un-normalised abundances, ratios for the specified conditions calculated from the normalised abundances, the corresponding p-values and adjusted p-values, number of unique peptides, q-values, PEP-values,  identification scores from both search engines."],"omics_type":["Proteomics"],"labhead":["Matt Hutchings"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Dept. Molecular Microbiology John Innes Centre Norwich Research Park Norwich, UK"],"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/PXD069151"],"additional_accession":[]},"is_claimable":false,"name":"The response regulator MtrA controls development through activation of bldM and whiI in Streptomyces venezuelae","description":"The response regulator MtrA is highly conserved in Streptomyces species where it coordinates antibiotic production with sporulation. Loss of MtrA results in a conditional bald phenotype in S. avermitilis, S. coelicolor and S. venezuelae, where the production of aerial hyphae and spores is blocked on some but not all growth media. In S. venezuelae NRRL-B-65442 ChIP-seq showed that MtrA binds to the promoters of >1000 genes including key genes required for development. Here we show that an S. venezuelae NRRL-B-65442 ∆mtrA mutant is bald on R2YE agar but develops normally on MYM agar. We used an in vitro DNA footprinting technique called Reusable DNA Capture Technology combined with Surface Plasmon Resonance (ReDCaT SPR) to identify the precise MtrA binding sites at the promoters of the developmental genes adpA, bldM, dnaA, filP, mtrA, ssgB and whiI. The results show that purified MtrA binds to single sites upstream of filP, mtrA, ssgB and whiI and to multiple sites upstream of adpA (x2), bldM (x5) and dnaA (x3) which may be indicative of the complex regulation of these genes. Tandem mass tag proteomics on the wild-type and ∆mtrA strains revealed that the levels of BldM and WhiI are 4-fold and 7-fold lower in the ∆mtrA mutant grown on R2YE agar suggesting they are directly regulated by MtrA under these growth conditions. They were not significantly affected in cultures grown on MYM agar. The expression of the key BldM and WhiI target genes ssgB, ssgR and whiB, which are key to development is also significantly reduced on R2YE agar. We conclude that MtrA directly activates expression of bldM and whiI on R2YE agar and that reduction in the levels of these regulators leads to the bald phenotype of the ∆mtrA mutant on this growth medium.","dates":{"publication":"2026-05-21","submission":"2025-10-06"},"accession":"PXD069151","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:112509","NEWT:475174","NEWT:111205","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:1907535","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:111225","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:37919","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:1538","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","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:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","N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