Extended Data Fig. 7: Structural characteristic analysis of proteins downregulated in RibosomeST-/- ESs.
From: A male germ-cell-specific ribosome controls male fertility
a, Downregulated proteins exhibited higher percentage of helix at amino acid positions of 10-11, 14-20, and 23-27 compared with unchanged proteins. Upregulated proteins exhibited a lower percentage of helix at amino acid positions from 23 to 38 compared with unchanged proteins. b, 3D structure of CCIN based on the AlphaFold Protein Structure Database (https://alphafold.ebi.ac.uk) with N-terminal 50 amino acids shown in blue, and the C-terminal half sequence shown in grey. c, Downregulated proteins formed more disulfide bonds in C-terminal half of the sequence than non-significance and upregulated proteins. d, 3D structure of CST13 based on the AlphaFold Protein Structure Database (https://alphafold.ebi.ac.uk) with N-terminal 50 amino acids coloured in blue, the C-terminal half sequence coloured in grey, and disulfide bonds are emphasized as red sticks. e, Amino acid enrichment analysis of upregulated proteins in RibosomeST-/- ESs. f, Levels of total thiols (P = 0.547) and glutathione (GSH) (P = 2.27 × 10−4) in RibosomeST-/- and wild-type N2a cell lines. n = 3. For a and f, data are mean ± s.e.m. P values were determined using two-sided Fisher’s exact tests for a; two-tailed Student’s t-tests for f. n values represent the number of independent experiments.
