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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 publication

DOI

10.1038/nchembio.1093

Type

Journal article

Journal

Nat Chem Biol

Publication Date

12/2012

Volume

8

Pages

960 - 962

Keywords

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