Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

• DOI: 10.1038/nchembio.1093
• Publication Date: 2012-10-29T14:36:17Z
• Authors: Wei Ge; Alexander Wolf; Tianshu Feng; Chia-hua Ho; Rok Sekirnik; Adam Zayer; Nicolas Granatino; Matthew E Cockman; Christoph Loenarz; Nikita D Loik; Adam P Hardy; Timothy D W Claridge; Refaat B Hamed; Rasheduzzaman Cho...; Lingzhi Gong; Carol V Robinson; David C Trudgian; Miao Jiang; Mukram M Mackeen; James S Mccullagh; Yuliya Gordiyenko; Armin Thalhammer; Atsushi Yamamoto; Ming Yang; Phebee Liu-Yi; Zhihong Zhang; Marion Schmidt-Za...; Benedikt M Kessler; Peter J Ratcliffe; Gail M Preston; Mathew L Coleman; Christopher J Sch...
• Keywords: Histone Demethylases; Ribosomal Proteins; 0301 basic medicine; Magnetic Resonance Spectroscopy; Chromosomal Proteins, Non-Histone; Escherichia coli Proteins; Nuclear Proteins; Arginine; Hydroxylation; Dioxygenases; Mixed Function Oxygenases; 3. Good health; 03 medical and health sciences; Prokaryotic Cells; Escherichia coli; Oxygenases; Animals; Humans; Histidine; Enzyme Inhibitors; Ribosomes

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.