The ubiquitous tripeptide Gly-Gly-Gln in class 1 polypeptide release factors triggers polypeptide release on ribosomes. The Gln residue in both bacterial and yeast release factors is N5-methylated, despite their distinct evolutionary origin. Methylation of eRF1 in yeast is performed by the heterodimeric methyltransferase (MTase) Mtq2p/Trm112p, and requires eRF3 and GTP. Homologues of yeast Mtq2p and Trm112p are found in man, annotated as an N6-DNA-methyltransferase and of unknown function. Here we show that the human proteins methylate human and yeast eRF1.eRF3.GTP in vitro, and that the MTase catalytic subunit can complement the growth defect of yeast strains deleted for mtq2.

• PMID: 18539146
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Reference Type

Journal Article | Research Support, Non-U.S. Gov't

Authors

Figaro S, Scrima N, Buckingham RH, Heurgué-Hamard V

Primary Lit For

MTQ2 | MTQ2-TRM112 eRF1 methyltransferase complex

Additional Lit For

SUP45 | TRM112 | ERF1-ERF3 translation release factor complex

Review For