Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

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 Chowdhury, Lingzhi Gong, Carol V Robinson, David C Trudgian, Miao Jiang, Mukram M Mackeen, James S McCullaghYuliya Gordiyenko, Armin Thalhammer, Atsushi Yamamoto, Ming Yang, Phebee Liu-Yi, Zhihong Zhang, Marion Schmidt-Zachmann, Benedikt M Kessler, Peter J Ratcliffe, Gail M Preston, Mathew L Coleman, Christopher J Schofield

Research output: Contribution to journalArticlepeer-review

98 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)960-2
Number of pages3
JournalNature Chemical Biology
Issue number12
Publication statusPublished - Dec 2012


  • Animals
  • Arginine
  • Chromosomal Proteins, Non-Histone
  • Enzyme Inhibitors
  • Escherichia coli
  • Histidine
  • Humans
  • Hydroxylation
  • Magnetic Resonance Spectroscopy
  • Nuclear Proteins
  • Oxygenases
  • Prokaryotic Cells
  • Ribosomal Proteins
  • Ribosomes


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