The post-translational modifications (PTMs) of ribosomes have been investigated in Saccharomyces cerevisiae and humans but have received little attention in other eukaryotic species. Methylation is notably present on ribosomal subunit proteins; there are 20 distinct methylation sites between humans and S. cerevisiae of which some are shared. However, the functions of ribosomal PTMs are largely unknown. Here we have investigated ribosomal proteins, from a range of eukaryotic species, to determine the PTMs present. The conservation of amino acids known to be methylated in humans or S. cerevisiae was first investigated via sequence comparison. Sites with methylated residues in humans or yeast were cross referenced with aligned sites in other eukaryotic species to determine if they were conserved, and hence whether the PTM of interest could be present. Methyltransferases of ribosome methylation sites were also checked for orthologs in such species. Secondly, a survey of site conservation across Eukarya and subclades was conducted using all species for which high quality sequences are available. This was done to assess the strength of site conservation in clades and hence when ribosome methylation of sites may have emerged. With a few exceptions sites were found to be strongly conserved across Eukarya. Mass spectrometry is also being used to discover ribosome PTMs. We intend to analyse a range of species such as Plasmodium falciparum (the malaria parasite), Arabidopsis thaliana (Mouse-ear cress), and Caenorhabditis elegans (a nematode species) and also those from extremophiles including a tardigrade and an Antarctic fungus. Subsequent to the identification of PTM sites we will investigate the responsible enzymes.