{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/msms.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/evidence.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/matchedFeatures.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/summary.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/peptides.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/modificationSpecificPeptides.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/parameters.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG7_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002731_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG9_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002735_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG12_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002741_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG14_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002745_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG3_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002723_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG5_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002727_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG10_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002737_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG11_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002739_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG8_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002733_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG13_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002743_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG15_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002747_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG2_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002721_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG16_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002749_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG4_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002725_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG6_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002729_JASK018_FL2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD070570/XG1_Proteome_F1_R1_T1_DDAOTIT001VNeoA_002719_JASK018_FL2.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["skotheim@stanford.edu"],"submitter":["Michael Lanz"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Cell gorwth","Yeast","Growth rate","Ribosomes"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070570"],"sample_protocol":["A 10 mL yeast culture (OD600=0.2) was harvested, snap-frozen, and stored at -80 °C. 1mM PMSF and protease inhibitors (1 tablet/10 mL) were then added to the lysis buffer (50 mM Tris-HCl pH 8.0, 0.2% Tergitol, 150 mM NaCl, 5 mM EDTA). Cells were then resuspended from in the lysis buffer, and lysed using a FastPrep-24 (4 °C, 5.5 m/s, 35 s). The lysate was then centrifuged (15,000 × g, 5 min, 4 °C) and the supernatant collected. SDS was then added to 1%, DTT to 5 mM, and the sample was incubated at 65 °C for 15 min. Then, 15 mM Iodoacetamide was added before incubation at room temperature for 15 min. Proteins were then precipitated by adding >3 volumes PPT solution (acetone:ethanol:acetic acid = 50%:49.9%:0.1%) folloed by incubation on ice for 15 min and centrifugation (17,000 × g, 5 min, 4 °C). The supernatant was discarded and the pellet washed with 500 µL PPT solution. The sample was then centrifuged again, the supernatant discarded, and the pellet was air dried for ~10 min. The pellet was then resuspended in fresh 75 µL urea/Tris solution (8M urea, 50 mM Tris-HCl pH=8.0) before adding 225 µL 150 mM NaCl solution. The sample was digested overnight at 37 °C with trypsin (1:50 enzyme:protein), with agitation. The next day, 15 µL 10% TFA (Trifluoroacetic acid) was added to stop digestion and the sample was centrifuged (17,000 × g, 2 min), and the supernatant recovered. The supernatant was then desalted using a C18 Cartridge (Waters #WAT054955). Aliquots were then stored at -20 °C. Desalted peptides were analyzed on a Fusion Lumos mass spectrometer (Thermo Fisher Scientific) equipped with a Thermo EASY-nLC 1200 LC system (Thermo Fisher Scientific)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["All raw files were searched using the Andromeda engine embedded in MaxQuant (v.2.4.2). Variable modifications included oxidation (M) and protein amino-terminal acetylation. Carbamidomethyl (C) was a fixed modification. The number of modifications per peptide was capped at five. Digestion was set to tryptic (proline blocked). MaxLFQ was used to determine the summed ion intensity for each protein. The database search was conducted using the UniProt proteome—Yeast_UP000002311_559292. The minimum peptide length was seven amino acids. The 1% false recovery rate (FDR) was determined using a reverse decoy proteome."],"omics_type":["Proteomics"],"labhead":["Jan Skotheim"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Stanford University"],"species":["Saccharomyces Cerevisiae (baker's Yeast)"],"publication":["Not available"],"submitter_mail":["mikelanz@stanford.edu"],"submitter_affiliation":["Stanford University"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Yeast growth is controlled by the proportional scaling of mRNA and ribosome concentrations","description":"Despite growth being fundamental to all aspects of cell biology, we do not yet know its organizing principles in eukaryotic cells. Classic models derived from the bacteria E. coli posit that protein-synthesis rates are set by mass-action collisions between charged tRNAs produced by metabolic enzymes and mRNA-bound ribosomes. These models show that faster growth is achieved by simultaneously raising both ribosome content and peptide elongation speed. Here, we test if these models are valid for eukaryotes by combining single-molecule tracking, spike-in RNA sequencing, and proteomics in 15 carbon- and nitrogen-limited conditions using the budding yeast S. cerevisiae. Ribosome concentration increases linearly with growth rate, as in bacteria, but the peptide elongation speed remains constant (~9 amino acids/s) and charged tRNAs are not limiting. Total mRNA concentration rises in direct proportion to ribosomes, driven by enhanced RNA polymerase II occupancy of the genome. We show that a simple kinetic model of mRNA-ribosome binding predicts both the fraction of active ribosomes, the growth rate, and responses to transcriptional perturbations. Yeast accelerate growth by coordinately and proportionally co-up-regulating total mRNA and ribosome concentrations, not by speeding elongation. Taken together, our work establishes a new framework for eukaryotic growth control and resource 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