Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

Nat Chem Biol. 2012 Dec;8(12):960-962. doi: 10.1038/nchembio.1093. Epub 2012 Oct 28.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arginine / metabolism
  • Chromosomal Proteins, Non-Histone / metabolism
  • Dioxygenases
  • Enzyme Inhibitors / pharmacology
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / antagonists & inhibitors
  • Escherichia coli Proteins / metabolism*
  • Histidine / metabolism
  • Histone Demethylases
  • Humans
  • Hydroxylation
  • Magnetic Resonance Spectroscopy
  • Mixed Function Oxygenases / antagonists & inhibitors
  • Mixed Function Oxygenases / metabolism*
  • Nuclear Proteins / metabolism
  • Oxygenases / antagonists & inhibitors
  • Oxygenases / metabolism*
  • Prokaryotic Cells / metabolism*
  • Ribosomal Proteins / metabolism
  • Ribosomes / metabolism*

Substances

  • Chromosomal Proteins, Non-Histone
  • Enzyme Inhibitors
  • Escherichia coli Proteins
  • Nuclear Proteins
  • RPL27A protein, human
  • Ribosomal Proteins
  • ribosomal protein L16
  • ribosomal protein L4
  • Histidine
  • Arginine
  • Mixed Function Oxygenases
  • Oxygenases
  • Dioxygenases
  • Histone Demethylases
  • RIOX2 protein, human
  • YcfD protein, E coli
  • RIOX1 protein, human

Associated data

  • PubChem-Substance/144220794
  • PubChem-Substance/144220795
  • PubChem-Substance/144220796
  • PubChem-Substance/144220797
  • PubChem-Substance/144220798
  • PubChem-Substance/144220799
  • PubChem-Substance/144220800
  • PubChem-Substance/144220801
  • PubChem-Substance/144220802
  • PubChem-Substance/144220803
  • PubChem-Substance/144220804
  • PubChem-Substance/144220805
  • PubChem-Substance/144220806
  • PubChem-Substance/144220807
  • PubChem-Substance/144220808
  • PubChem-Substance/144220809