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Ten µg of a 1:1 mixture of hydrophilic and hydrophobic carboxyl-coated paramagnetic beads (SeraMag, #24152105050250 and #44152105050250, GE Healtcare) were added for each µg of protein. Protein binding was induced by addition of acetonitrile to a final concentration of 50% (v/v). Samples were incubated for 10 minutes at room temperature. The tubes were placed on a magnetic rack and beads were allowed to settle for three minutes. The supernatant was discarded and beads were rinsed three times with 200 µL of 80% ethanol without removing the tubes from the rack. Beads were resuspended in digestion buffer containing 50 mM triethylammmoniumbicarbonate and both Trypsin (Serva) and Lys-C (Wako) in a 1:50 enzyme to protein ratio. Protein digestion was carried out for 14 hours at 37°C in a PCR cycler. Afterwards the supernatant was recovered dried down in a vacuum concentrator.   Mass spectrometry All samples were analyzed on a Orbitrap Exploris (Thermo Scientific) equipped with a FAIMS Pro device and coupled to a 3000 RSLC nano UPLC (Thermo Scientific). Samples were loaded on a pepmap trap cartridge (300 µm i.d. x 5 mm, C18, Thermo) with 2% acetonitrile, 0.1% TFA at a flow rate of 20 µL/min. Peptides were separated over a 50 cm analytical column (Picofrit, 360 µm O.D., 75 µm I.D., 10 µm tip opening, non-coated, New Objective) that was packed in-house with Poroshell 120 EC-C18, 2.7 µm (Agilent). Solvent A consists of 0.1% formic acid in water. Elution was carried out at a constant flow rate of 300 nL/min using a 60 minute method: 8-30% solvent B (0.1% formic acid in 80% acetonitrile) within 23 minutes, 30-45% solvent B within 3 minutes, 45-98% buffer B within 0.5 minute, followed by column washing and equilibration. Data acquisition on the Orbitrap Exploris was carried out using a data-dependent method in positive ion mode. MS survey scans were acquired from 375-1500 m/z in profile mode at a resolution of 60,000. AGC target was set to 200% at a maximum injection time of 25 ms. Peptides with charge states 2-6 were isolated within a window of 1.2 m/z and subjected to HCD fragmentation at a normalized collision energy of 27%. The MS2 AGC target was set to 200%, allowing a maximum injection time of 22 ms. Product ions were detected in the Orbitrap at a resolution of 15,000. Precursors were dynamically excluded for 20 s. The cycle time was set to 1 s for each of the two FAIMS voltages of −45 and −65 V."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["Raw files were processed with MSFragger v3.5 using the default settings. Briefly, peak lists were extracted from raw files and searched using against a Uniprot Bacillus subtilis database (version 220530, taxonomy ID 224308) and a database containing sequences of common contaminants and decoys. Trypsin/P was set as enzyme specificity, allowing a maximum of two missed cleavages. Peptide matches were filtered to 1% FDR using PeptideProphet and Philosopher (version 4.4.0). Further data processing was carried out in R and Perseus."],"omics_type":["Proteomics"],"labhead":["Kathirvel Alagesan"],"instrument_platform":[""],"labhead_affiliation":["Max Planck Unit for the Science of Pathogens Charitéplatz 1,D-10117 Berlin, Germany"],"submission_type":["PARTIAL"],"species":["Bacillus Subtilis"],"publication":["Not available"],"submitter_mail":["alagesan@mpusp.mpg.de"],"submitter_affiliation":["Max Planck Unit for the Science of Pathogens"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Stress-induced ribosome degradation in Bacillus subtilis is mediated by the RNase Y-specificity complex","description":"Limiting the synthesis and activity of ribosomes is crucial for responding to various stresses, including nutrient starvation or proteotoxic stress. In Bacillus subtilis, this is achieved through the coordinated action of the alarmones (p)ppGpp and the transcription factor Spx. In this study, we performed a genetic screening for new factors involved in the heat shock response of B. subtilis. We discovered that the RNase Y specificity factor Y-complex is important for the heat shock response and the transition to the stationary growth phase. The Y-complex is required for processing different RNAs, including mRNA maturation. We further demonstrate that the Y-complex and RNase Y initiate rRNA degradation in mature ribosomes, lowering their abundance. We propose the Y-complex as a system by which B. subtilis regulates protein synthesis and resource allocation at the entry to stationary 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