As inferred from homologues in Saccharomyces cerevisiae, TRMT11 (catalytic subunit) and TRMT112 (zinc-binding subunit) form a complex which methylates the 2 position of guanosine-10 in tRNA (Purushothaman et al. 2005).
Inorganic arsenic (iAs) compounds are human carcinogens. The most toxic arsenic metabolite is monomethylarsonous acid (MMAIII). Arsenic (3+) methyltransferase (AS3MT) is the primary enzyme responsible for methylating MMAIII to the less toxic dimethylarsonic acid (DMAA). A human ortholog of yeast MTQ2, HemK methyltransferase family member 2 (aka N(6)-adenine-specific DNA methyltransferase 1, N6AMT1), is also able to methylate MMAIII using S-adenosyl L-methionine as methyl donor (Ren et al. 2011). N6AMT1 forms a heterodimer with multifunctional methyltransferase subunit TRM112-like protein (TRMT112) (Figaro et al. 2008).
Class 1 release factors such as eukaryotic peptide chain release factor subunit 1 (ETF1) direct the termination of peptide translation in response to the termination codons UAA, UAG and UGA. ETF1 needs to be complexed with ERF3 in its GTP-bound form to be efficiently post-translationally methylated. HemK methyltransferase family member 2 (N6AMT1) is a heterodimeric methyltransferase that catalyses N5-methylation of ETF1 on glutamine 185 (Q185), using S-adenosyl L-methionine (AdoMet) as the methyl donor (Figaro et al. 2008). N6AMT1 forms a complex with multifunctional methyltransferase subunit TRM112-like protein (TRMT112)
The WBSCR22:TRMT112 complex, homolog of the Bud23:Trm112 complex in yeast (Ounap et al. 2013), methylates guanosine-1639 of 18S rRNA at the N(7) position of the guanine base (Haag et al. 2015, Zorbas et al. 2015). The WBSCR22:TRMT112 complex but not its methylase activity is required for efficient processing of precursor rRNA at site 2 and site 3 (Haag et al. 2015, Zorbas et al. 2015). Hemizygosity at the region containing WBSCR22 causes Williams-Beuren syndrome (Doll and Grzeschik 2001).