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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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter 2-oxoglutarate Oxygenase ; Hypoxia ; Ribosome ; Translational Control
Sprache englisch
Veröffentlichungsjahr 2014
HGF-Berichtsjahr 2014
ISSN (print) / ISBN 0027-8424
e-ISSN 1091-6490
Zeitschrift Proceedings of the National Academy of Sciences of the United States of America
Quellenangaben Band: 111, Heft: 11, Seiten: 4031-4036 Artikelnummer: , Supplement: ,
Verlag National Academy of Sciences
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Molecular Toxicology and Pharmacology (TOX)
POF Topic(s) 30504 - Mechanisms of Genetic and Environmental Influences on Health and Disease
Forschungsfeld(er) Enabling and Novel Technologies
PSP-Element(e) G-552500-001
PubMed ID 24550447
DOI 10.1073/pnas.1314482111
Scopus ID 84896511439
Erfassungsdatum 2014-03-20
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