Fig. 2: Translational buffering maintains a largely stable protein expression in 2iL ESCs.

a Venn diagram showing the overlap between RNAs, RFPs, and proteins detected in SL, 2iL, or EPI states. RNAs with minimum of 50 reads and RFP with minimum of 25 reads in at least one of the ES conditions were selected and intersected with the 5969 detected proteins. Only uniquely annotated proteins that could be detected in all three conditions (to allow for fold change comparison) were maintained, giving rise to n = 3294 uniquely assigned RFP–RNA–protein IDs. b Scatter plot showing the correlation between fold change in RFP, RNA, and proteins when SL or EPI are compared to 2iL state. Values represent the mean of two highly similar biological replicates. n = 3924 RFP–RNA–protein IDs. R-values represent Pearson correlation coefficients. c Scatter plot showing the correlation between changes in TE and protein expression when SL or EPI are compared to 2iL state. Values represent the mean of two highly similar biological replicates. n = 3924 RFP–RNA–protein IDs. r-values represent Pearson correlation coefficients. d Box plots showing the opposite changes in RNAs and RFPs abundances that result in maintenance of constant protein levels in different states of ESCs and during the SL-to-2iL or 2iL-to-SL transition. Box=25–75th percentile; bar=median; whiskers=5–95th percentile. e Bar plot showing the fold change in RNA-, RFP-, and protein-levels of Rnf126 during 2iL-to-SL transition and in EPI state. f Bar plot showing the distribution of Rnf126 mRNAs in low-density and high-density polysome fractions in different states of ESCs. The qRT-PCR values represent the mean of two highly similar biological replicates. g Western blot analysis of RNF126 in different ESC states. Two biological replicates were used per condition.