Nhan van Tran, Felix G M Ernst, Ben R Hawley, Christiane Zorbas, Nathalie Ulryck, Philipp Hackert, Katherine E Bohnsack, Markus T Bohnsack, Samie R Jaffrey, Marc Graille and Denis L J Lafontaine
Nucleic Acids Res. (2019). doi:10.1093/nar/gkz619
In this study, the authors identify METTL5 as the enzyme responsible for 18S rRNA m6A modification, demonstrate the involvement of the TRMT112 methyltransferase activator protein in its stabilization and activity, and determine the structure of the enzyme-activator complex. The study also confirms a recently described, analogous role for ZCCHC4 as a 28S rRNA m6A modification enzyme. The role of TRMT112 in stabilising METTL5, previously unknown, has important implications for future work that will determine how stabilising subunits affect the mechanism of the enzyme.