Singleton RS., Liu-Yi P., Formenti F., Ge W., Sekirnik R., Fischer R., Adam J., Pollard PJ., Wolf A., Thalhammer A., Loenarz C., Flashman E., Yamamoto A., Coleman ML., Kessler BM., Wappner P., Schofield CJ., Ratcliffe PJ., Cockman ME.

Significance Members of the 2-oxoglutarate (2OG)-dependent oxygenase superfamily catalyze a range of important biological oxidations. Structurally informed bioinformatic predictions suggest that the human genome encodes as yet unassigned members of the superfamily. We describe work demonstrating that 2OG and Fe(II)-dependent oxygenase domain-containing protein 1 (OGFOD1) is a protein hydroxylase that modifies the small ribosomal subunit protein RPS23 at a conserved prolyl residue in the ribosome-decoding center and that suppression or deletion of OGFOD1 is associated with the activation of translational stress pathways. Together with studies of homologous genes in flies and yeast described in accompanying manuscripts, the work identifies a unique function for 2OG oxygenase-catalyzed hydroxylation in ribosome biology.

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

Singleton RS., Liu-Yi P., Formenti F., Ge W., Sekirnik R., Fischer R., Adam J., Pollard PJ., Wolf A., Thalhammer A., Loenarz C., Flashman E., Yamamoto A., Coleman ML., Kessler BM., Wappner P., Schofield CJ., Ratcliffe PJ., Cockman ME.

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