Tara K. Bartolec

Abstract Bacteria and bacteriophages are in a constant arms race to develop defence and anti-defence systems, respectively. Currently known phage-encoded anti-defence systems are specific to the activity of the targeted bacterial defence system. Here we identify a mechanism by which the T7 bacteriophage broadly counteracts bacterial defences using protein phosphorylation.

Keywords ribosome translation lysine methylation methyltransferase substrate specificity Research topic(s) CP: Molecular biology Introduction For over half a century, it has been known that the eukaryotic protein translational machinery is highly modified by protein methylation.1 Only in the last two decades, however, have enzymes catalyzing the methylation of ribosomes and translation factors been discovered.

Abstract The eukaryotic ribosome is highly modified by protein methylation, yet many of the responsible methyltransferases remain unknown. Here we have identified SMYD5 as a ribosomal protein methyltransferase that catalyses trimethylation of RPL40/eL40 at lysine 22. Through a systematic mass spectrometry-based approach, we show that the human ribosome has 12 primary sites of protein methylation, including at RPL40 K22.