OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation.

Research output: Contribution to journalArticle


  • rachelle singleton
  • P Liu-Yi
  • F Formenti
  • Wei Ge
  • Rok Sekirnik
  • Fischer R
  • Julie Adam
  • Patrick Pollard
  • Alex Wolf
  • A Thalhammer
  • Christoph Loenarz
  • Emily Flashman
  • Benedikt Kessler
  • pablo wappner
  • Christopher J Schofield
  • Peter J Ratcliffe
  • Matthew E Cockman

Colleges, School and Institutes

External organisations

  • University of Oxford
  • Leloir Institute Foundation


2-Oxoglutarate (2OG) and Fe(II)-dependent oxygenase domain-containing protein 1 (OGFOD1) is predicted to be a conserved 2OG oxygenase, the catalytic domain of which is related to hypoxia-inducible factor prolyl hydroxylases. OGFOD1 homologs in yeast are implicated in diverse cellular functions ranging from oxygen-dependent regulation of sterol response genes (Ofd1, Schizosaccharomyces pombe) to translation termination/mRNA polyadenylation (Tpa1p, Saccharomyces cerevisiae). However, neither the biochemical activity of OGFOD1 nor the identity of its substrate has been defined. Here we show that OGFOD1 is a prolyl hydroxylase that catalyzes the posttranslational hydroxylation of a highly conserved residue (Pro-62) in the small ribosomal protein S23 (RPS23). Unusually OGFOD1 retained a high affinity for, and forms a stable complex with, the hydroxylated RPS23 substrate. Knockdown or inactivation of OGFOD1 caused a cell type-dependent induction of stress granules, translational arrest, and growth impairment in a manner complemented by wild-type but not inactive OGFOD1. The work identifies a human prolyl hydroxylase with a role in translational regulation.


Original languageEnglish
Pages (from-to)4031
Number of pages6
JournalNational Academy of Sciences. Proceedings
Issue number11
Publication statusPublished - 18 Mar 2014