PuSH - Publikationsserver des Helmholtz Zentrums München: OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation.

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Singleton, R.S.* ; Liu-Yi, P.* ; Formenti, F.* ; Ge, W.* ; Sekirnik, R.* ; Fischer, R.* ; Adam, J.* ; Pollard, P.J.* ; Wolf, A. ; Thalhammer, A.* ; Loenarz, C.* ; Flashman, E.* ; Yamamoto, A.* ; Coleman, M.L.* ; Kessler, B.M.* ; Wappner, P.* ; Schofield, C.J.* ; Ratcliffe, P.J.* ; Cockman, M.E.*

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

Proc. Natl. Acad. Sci. U.S.A. 111, 4031-4036 (2014)

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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.

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