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Peptides were loaded onto a PepMap trap cartridge (300 µm i.d. x 5 mm, C18, Thermo) with 2% acetonitrile and 0.1% TFA at a 20 µL/min flow rate. 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 250 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. The mass spectrometer was operated in data-independent acquisition (DIA) and positive ionization mode. MS1 full scans (375–1500 m/z) were acquired with a resolution of 60,000, a normalized automatic gain control target value of 120%, and a maximum injection time set to 55 ms. Peptide fragmentation was performed using higher energy collision-induced dissociation and a normalized collision energy of 30%. MS2 spectra were acquired with a resolution of 30,000 (first mass 100 m/z) with 8 m/z DIA windows between 400 and 1200 m/z. A normalized automatic gain control target value of 100%, and a maximum injection time of 54 ms."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["DIA-NN (DIA-NN 1.8.1) was employed for DIA data analysis. The main DIA-NN report “report.txt” was used for all calculations. Fasta file (Bacillus_subtilis_Strain168_UP000001570.fasta) was digested with a maximum of one missed cleavage. Peptide length was restricted from 7 to 30 peptides, and the precursor m/z range was set from 300 to 1800. N-terminal methionine excision was enabled. Cysteine carbamidomethylation was selected as a fixed modification, and methionine oxidation and N-terminal acetylation as variable modifications. The maximum number of variable modifications was set to two. All other parameters were default settings, including the 1% precursor FDR and enabled match between runs (MBR). The main DIA-NN report “report.pg_matrix.tsv” was used for all calculations."],"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":"Targeting the translation machinery: The RNase Y specificity factor Y-complex coordinates ribosome degradation","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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