| Literature DB >> 23103944 |
Wei Ge1, Alexander Wolf1, Tianshu Feng2, Chia-Hua Ho1, Rok Sekirnik1, Adam Zayer2, Peter J Ratcliffe2, Gail M Preston3, Mathew L Coleman2, Christopher J Schofield1, Nicolas Granatino1, Matthew E Cockman2, Christoph Loenarz1, Nikita D Loik1, Adam P Hardy1, Timothy D W Claridge1, Refaat B Hamed1, Rasheduzzaman Chowdhury1, Lingzhi Gong1, Carol V Robinson1, David C Trudgian4, Miao Jiang1, Mukram M Mackeen1, James S Mccullagh1, Yuliya Gordiyenko1, Armin Thalhammer1, Atsushi Yamamoto2, Ming Yang2, Phebee Liu-Yi2, Zhihong Zhang1, Marion Schmidt-Zachmann5, Benedikt M Kessler2.
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.Entities:
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Year: 2012 PMID： 23103944 PMCID： PMC4972389 DOI： 10.1038/nchembio.1093
Source DB: PubMed Journal: Nat Chem Biol ISSN： 1552-4450 Impact factor: 15.040