Prideapplication/xmlftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD053764/20220228-proteomics-experiment.zipftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD053764/txt-proteomics.zipftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD053764/txt-Phospho.zipftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/09/PXD053764/20220303-phospho-experiment.zipprimaryOK200matthias.trost@ncl.ac.ukMatthias TrostData-dependent acquisitionMass SpectrometryBottom-up proteomicsStreptomyces albushttps://www.ebi.ac.uk/pride/archive/projects/PXD053764Peptide clean-up for Phosphopeptide enrichment and LC-MS injection Peptides after in-solution digestion were acidified with 10% TFA, to bring the pH <3. The samples were diluted with 3% acetonitrile in 0.1% TFA. C18 spin-columns were used for sample clean-up. Briefly, the column was activated with 100% MeOH, followed by equilibration with 3% acetonitrile in 0.1% TFA. Sample was bound on the equilibrated column followed by 5 washes with 3% acetonitrile in 0.1% TFA. The bound peptides were then eluted with 60% Acetonitrile in 0.1% TFA and the samples were freeze dried in a lyophilizer. The dried sample were stored at -80°C until further use. Phosphopeptide Enrichment Phosphopeptide enrichment was performed with 495 µg of peptides for each replicate. In-house TiO2 based enrichment method was used. Briefly, Peptides were reconstituted in 250mM lactic acid/3% TFA/70% can. The TiO2 slurry is used to make in-house enrichment micro-columns. The micro columns are equilibrated with 3% TFA/70% ACN before binding the peptides on the column. The sample is then washed to remove non-phosphorylated peptides. Phosphopeptides are then eluted using 1% NH4OH in a fresh tube and dried in a freeze dryer immediately and stored at -80°C. LC/MS Injection The phosphopeptides were reconstituted in 5µL of 0.1% formic acid and vortexed, sonicated and centrifuged at 14000xg before injecting on the Mass Spectrometer where 2 µL was injected into the mass spectrometer. Peptides were analysed by nanoflow-LC-MS/MS using timsTOF Pro2 (Bruker) coupled to a nanoElute liquid chromatography device (Bruker). Samples were injected on a 100 μm ID × 5mm trap (Thermo Trap Cartridge 5mm) and separated on a 75 μm × 15 cm nano LC column (BrukerFIFTEEN part# 184262). All solvents used were HPLC or LC-MS Grade (Fluka™). Peptides were loaded on the trap for 2 minutes at constant pressure of 217 bar using 0.1% FA, in Water. The separation column was conditioned using 100% Buffer A (0.1% FA, in Water) at 800bar constant for 3 min and the separation was performed on a linear gradient from 2 to 25 % Buffer B (0.1% FA in Acetonitrile) over 35 minutes at 300 nL/min. The column was then washed with 90% Buffer B for 5 minutes and equilibrated 10 minutes with 100% Buffer A in preparation for the next analysis. Full MS scans were acquired from m/z 100 to m/z 1700 at resolution 38000 in DDA-PASEF mode. The Ion mobility(1/K0) was measured at a range between 0.78-1.6 V.s/cm2 where both the Ramp time and Accumulation time for the TIMS device was set to 100ms. The duty cycle was performed at 100% at a ramp rate of 9.43 Hz. The same settings were used for total proteomic experiment, where each sample was injected at a concentration of 100ng/µL.PrideData Analysis Peptide Identification was carried out with MaxQuant (version 1.6.10.43). MS/MS spectra were searched against database provided earlier (“Proteins for J1074_NCBI”) using a false discovery rate of 1%. The maximum of missed cleavage was set to 2 using Trypsin/P enzyme. Carbamidomethylation (C) was set as fixed modification and acetylation (Protein N term), oxidation (M), Phospho (STY), were set as variable modifications. The data was further analysed using a combination or R and Perseus.ProteomicsMatthias TrostPARTIALNewcastle University Biosciences Institute, Faculty of Medical Sciences, Newcastle upon Tyne, NE2 4HH, UKBacteriaStreptomyces Albus42265934 Derkacz M, Watson A, Gajbhiye A, Tracz M, Jakimowicz D, Trost M, Errington J, Kepplinger B. Roles of PknB and CslA in Cell Wall Morphogenesis of Streptomyces. Mol Microbiol. 2026 126(2):161-172 10.1111/mmi.70086matthias.trost@ncl.ac.ukNewcastle UniversityUnited KingdomThe bacterial cell wall is essential for maintaining cellular integrity and defining the mode of growth, with different species adopting distinct strategies for cell wall synthesis and remodelling. Streptomyces are filamentous bacteria predominantly found in soil and renowned for producing specialised metabolites, including antibiotics. They grow through tip extension and branching hyphal filaments, forming a multicellular mycelium. New branches are established by forming a new growth zone on the lateral cell wall. Proteins involved in this process are organised into complexes called polarisomes, with DivIVA being the most well-characterised component. To investigate the tip growth requirements in Streptomyces albus we developed a genetic screen utilising toxic DivIVA overproduction and searched for suppressors of its lethality, reasoning that such suppressors would likely encode components functionally linked to DivIVA or the tip growth machinery. Among the identified genes was pknB, encoding a serine/threonine protein kinase implicated in the regulation of cell growth and morphogenesis. We confirmed that deletion of pknB restored the growth phenotype of S. albus following DivIVA overproduction. The phosphoproteome analysis revealed that the absence of PknB alters the phosphorylation state of CslA, a cellulose synthase that synthesizes a beta-glucan (cellulose) polymer. We demonstrate that a phosphoablative mutant of CslA impairs beta-glucan synthesis and causes hypersensitivity to lysozyme. Overproduction of CslA restored colony growth defects arising from DivIVA-induced hyperbranching, without however suppressing the hyperbranching phenotype. These findings collectively identify PknB-dependent phosphorylation of CslA as a central regulatory point in Streptomyces cell envelope construction, revealing how modulation of beta-glucan synthesis can mitigate the cellular consequences of DivIVA dysregulation.Roles of PknB and CslA in Cell Wall Morphogenesis of Streptomyces.Derkacz Marta M, Watson Andrew A, Gajbhiye Akshada A, Tracz Michał M, Jakimowicz Dagmara D, Trost Matthias M, Errington Jeff J, Kepplinger Bernhard BfalseThe kinase PknB modulates the cell wall biosynthetic machineryStreptomyces are filamentous bacteria living mostly in the soil and best known for their ability to produce specialised metabolites (e.g. antibiotics). They grow as tip-extending, branching hyphal filaments to form a multicellular mycelium. New branches are established by the formation of a new growth zone on the lateral cell wall. Proteins responsible for this process are organised in complexes called polarisomes, with DivIVA being the best described component. We have developed a genetic screen based on DivIVA overexpression to identify proteins potentially interacting with DivIVA in Streptomyces albus. Among the hits was the important morphogenic genes encoding PknB (Ser/Thr kinase). We confirmed that deletion of pknB rescues S. albus from the effects of overexpressing DivIVA. Next, we studied the impact of pknB deletion in Streptomyces. A mass spectrometry phosphoproteome analysis indicated that absence of PknB alters the phosphorylation state of CslA, a cellulose synthase-like protein, containing a transglycosylase domain. Our research demonstrated that a phosphoablative mutant of CslA impacts its activity in β-glucan synthesis, as it displays a similar hypersensitivity to lysozyme as a CslA deletion strain. This highlights one pathway through which PknB affects the stability of the cell wall structure and possibly explains its impact in rescuing the cell from a lethal overproduction of DivIVA. Our findings highlight the role of PknB in maintaining the cellular structure and integrity of the Streptomyces cell 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