Evolutionary Origins and Functional Diversification of 2'-O-Methyltransferases: Insights from Phylogenetic and Structural Analysis.

ABSTRACT: Ribose 2'-O-methylation (Nm), a key RNA modification, is catalyzed by diverse 2'-O-methyltransferases (2'-O-MTases), yet the evolutionary trajectories of these enzymes remain poorly studied. Here, with a comprehensive collection of functionally validated 2'-O-MTases, we classified them into 11 families based on the distinct methyltransferase (MTase) domains. Homology searches across 198 species identified 6746 proteins, revealing the widespread distribution of 2'-O-MTases across the Tree of Life. Eight MTase domains (e.g., FtsJ, SpoU-methylase) existed both in eukaryotes and prokaryotes, indicating their ancient origin in the Last Universal Common Ancestor (LUCA). In contrast, the AdoMet-MTase, TRM13, and Trm56 domains are lineage-specific. Copy number expansion of most 2'-O-MTase families

SUBMITTER: Wang SN 

PROVIDER: S-EPMC12155479 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature