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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans.
- Source :
-
Nature chemical biology [Nat Chem Biol] 2012 Dec; Vol. 8 (12), pp. 960-962. Date of Electronic Publication: 2012 Oct 28. - Publication Year :
- 2012
-
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.
- Subjects :
- Animals
Arginine metabolism
Chromosomal Proteins, Non-Histone metabolism
Dioxygenases
Enzyme Inhibitors pharmacology
Escherichia coli metabolism
Escherichia coli Proteins antagonists & inhibitors
Histidine metabolism
Histone Demethylases
Humans
Hydroxylation
Magnetic Resonance Spectroscopy
Mixed Function Oxygenases antagonists & inhibitors
Nuclear Proteins metabolism
Oxygenases antagonists & inhibitors
Ribosomal Proteins metabolism
Escherichia coli Proteins metabolism
Mixed Function Oxygenases metabolism
Oxygenases metabolism
Prokaryotic Cells metabolism
Ribosomes metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1552-4469
- Volume :
- 8
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Nature chemical biology
- Publication Type :
- Academic Journal
- Accession number :
- 23103944
- Full Text :
- https://doi.org/10.1038/nchembio.1093