Structural insights into the specific recognition of mitochondrial ribosome-binding factor hsRBFA and 12 S rRNA by methyltransferase METTL15.

ABSTRACT: Mitochondrial rRNA modifications are essential for mitoribosome assembly and its proper function. The m⁴C methyltransferase METTL15 maintains mitochondrial homeostasis by catalyzing m⁴C839 located in 12 S rRNA helix 44 (h44). This modification is essential to fine-tuning the ribosomal decoding center and increasing decoding fidelity according to studies of a conserved site in Escherichia coli. Here, we reported a series of crystal structures of human METTL15-hsRBFA-h44-SAM analog, METTL15-hsRBFA-SAM, METTL15-SAM and apo METTL15. The structures presented specific interactions of METTL15 with different substrates and revealed that hsRBFA recruits METTL15 to mitochondrial small subunit for further modification instead of 12 S rRNA. Finally, we found that METTL15 deficien

SUBMITTER: Lv M 

PROVIDER: S-EPMC10828496 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature