PuSH - Publication Server of Helmholtz Zentrum München

Export: TXT Text RIS Endnote (RIS) BIB BibTeX
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)
Publ. Version/Full Text Volltext DOI PMC
Open Access Gold
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.
Impact Factor
Scopus SNIP
Web of Science
Times Cited
Scopus
Cited By
Altmetric
9.809
2.734
35
31
Tags
Annotations
Special Publikation
Hide on homepage

Edit extra information
Edit own tags
Private
Edit own annotation
Private
Hide on publication lists
on hompage
Mark as special
publikation
Publication type Article: Journal article
Document type Scientific Article
Keywords 2-oxoglutarate Oxygenase ; Hypoxia ; Ribosome ; Translational Control
Language english
Publication Year 2014
HGF-reported in Year 2014
ISSN (print) / ISBN 0027-8424
e-ISSN 1091-6490
Journal Proceedings of the National Academy of Sciences of the United States of America
Quellenangaben Volume: 111, Issue: 11, Pages: 4031-4036 Article Number: , Supplement: ,
Publisher National Academy of Sciences
Reviewing status Peer reviewed
Institute(s) Institute of Molecular Toxicology and Pharmacology (TOX)
POF-Topic(s) 30504 - Mechanisms of Genetic and Environmental Influences on Health and Disease
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-552500-001
PubMed ID 24550447
DOI 10.1073/pnas.1314482111
Scopus ID 84896511439
Erfassungsdatum 2014-03-20
[➜Report correction]