Riboproteome remodelling during quiescence exit in Saccharomyces cerevisiae

Published: 10 November 2023| Version 1 | DOI: 10.17632/sx57cnnb4p.1
Paula Portela


Characterization of the riboproteome composition in quiescent cells and post-translational reactivation. To characterize ribosome heterogeneity during the exit from quiescence, the protein composition of ribosomal particles from stationary phase and nutrient-stimulated cells was assessed using a label-free quantitative mass spectrometry strategy.. To this end, crude extracts from these cells were subjected to sucrose gradient centrifugation and three fractions free (F); monosome (M=80S + 60S + 40S) and polysome (P) were analyzed by nano-HPLC-MS/MS. A total of 528 proteins were identified. Supplemenary Table 1 contains Protein content (M%) mean and standard error. n:=3 biological replicates for each fraction/condition; Log Poly-Mono PR abundance: mean and standard error of log (P/M) PR abundance from the log (protein abundance M% polysome sample x/protein abundance M% and Co-fractionated protein distribution F, M, P= ln M% fraction/((M%Free+M%Monosome+M%Polysome)/3)). The color scale indicates the level of protein distribution between F (free), M (monosome) and P (polysome) fraction. Bold values represent values greater than 0.74 on the co-fractionated protein distribution free, monosome, and polysome index (proteins exhibiting a high concentration in a unique fraction accumulating over 70%). Supplementry Table 2 contains the normalized ribosomal protein abundance.



Universidad de Buenos Aires


Mass Spectrometry, Ribosome, Saccharomyces cerevisiae