Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans.
Ge W., Wolf A., Feng T., Ho CH., Sekirnik R., Zayer A., Granatino N., Cockman ME., Loenarz C., Loik ND., Hardy AP., Claridge TDW., Hamed RB., Chowdhury R., Gong L., Robinson CV., Trudgian DC., Jiang M., Mackeen MM., Mccullagh JS., Gordiyenko Y., Thalhammer A., Yamamoto A., Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M., Kessler BM., Ratcliffe PJ., Preston GM., Coleman ML., Schofield CJ.
The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and prokaryotic proteins are analogously modified. Escherichia coli ycfD is a growth-regulating 2-oxoglutarate oxygenase catalyzing arginyl hydroxylation of the ribosomal protein Rpl16. Human ycfD homologs, Myc-induced nuclear antigen (MINA53) and NO66, are also linked to growth and catalyze histidyl hydroxylation of Rpl27a and Rpl8, respectively. This work reveals new therapeutic possibilities via oxygenase inhibition and by targeting modified over unmodified ribosomes.