Fig. 2

DNA methylation machinery is conserved and differentially expressed across different tissues. Phylogenetic trees of A DNMT1 and B UHRF1 in a representative subset of 19 metazoan and outgroup species. Colors indicate phyla (blue = Chordata; pink = Mollusca; orange = Porifera), and octopus are indicated with an icon. C DNMT1 domain structure in H. sapiens and O. bimaculoides. Numbers indicate amino acid residues for each species. D Alignment of the C-terminal Catalytic Domain (CTD) of O. bimaculoides to M. musculus, H. sapiens, and D. rerio shows that the major residue needed for DNMT1 catalytic function is highly conserved among the species. Residue functionality was assigned based on the mouse DMNT1 ortholog. E Domain structure of UHRF1 in H. sapiens and O. bimaculoides. F Alignment of the O. bimaculoides SRA domain to M. musculus, H. sapiens, and D. rerio shows that all major residues needed for UHRF1 functionality are conserved among the species. Residue functionality is based on the mouse UHRF1 ortholog. Alignment to UHRF2 shows no conservation of the critical residues between the SRA domain in O. bimaculoides and UHRF2 in H. sapiens and M. musculus. G Structural superposition of the 3D structure of BAH1, BAH2, and CTD domains in M. musculus (grey) with the 3D model of the same domains in O. bimaculoides (red). DNA is represented in brown, and critical residues for 5mC deposition are highlighted in red. H Structural superposition of the 3D structure of the SRA domain in M. musculus (grey) with the 3D model of the same domain in O. bimaculoides (green). DNA is represented in brown and residues critical for CpGs recognition and 5mC base flipping are highlighted in red. I Expression profiles of DNA methylation machinery. Gene names are extracted from Trinotate (Table S6)