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[Preprint]. 2023 Jul 10:2023.07.10.548325. [Version 1] doi: 10.1101/2023.07.10.548325

Figure 5: The Ltv1_L216S mutation globally disrupts head assembly.

Figure 5:

(A) Mature ribosomes from yeast expressing wt Ltv1 or Ltv1_L216S were purified and analyzed by mass spectrometry. Spectral counts for each protein in each sample were normalized by the total number of spectra, and abundance of each protein in Ltv1_L216S ribosomes normalized by the abundance in wt Ltv1 ribosomes. Number of spectra for each protein are indicated on the far left. Ribosomal proteins are color-coded for the substructure to which they bind, with head-binding proteins in blue, platform proteins in green, and proteins from the body in yellow. Averaged data from three biological replicates are shown. (B) Structure of mature 40S ribosomes highlighting the different substructures with the same color-code as in (A). (C) Western analysis of ribosomes purified from cells expressing Rps29-HA and either wt Ltv1 or Ltv1_L216S. Rps29 occupancy was quantified relative to Rps2 and Rps0. Significance was tested using an unpaired t-test. **, P<0.01; ****, P<0.0001.