Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans
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Wei Ge Alexander Wolf Tianshu Feng Chia-hua Ho Rok Sekirnik Adam Zayer Nicolas Granatino Matthew Cockman Christoph Loenarz Nikita D Loik Adam P Hardy Timothy DW Claridge Refaat B Hamed Rasheduzzaman Chowdhury 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-Zachmann Benedikt M Kessler Peter Ratcliffe Gail M Preston Mathew L Coleman Christopher J Schofield
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Abstract
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.
Journal details
Journal
Nature Chemical Biology
Volume
8
Issue number
12
Pages
960-962
Publication date
Full text links
Publisher website (DOI)
10.1038/nchembio.1093
Europe PubMed Central
23103944
Pubmed
23103944
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