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dc.creatorSingleton, Rachelle S.-
dc.creatorLiu Yi, Febee-
dc.creatorFormenti, Fabio-
dc.creatorGe, Wei-
dc.creatorSekirnik, Rok-
dc.creatorFischer, Roman-
dc.creatorAdam, Julie-
dc.creatorPollard, Patrick J.-
dc.creatorWolf, Alexander-
dc.creatorThalhammer, Armin-
dc.creatorLoenarz, Christoph-
dc.creatorFlashman, Emily-
dc.creatorYamamoto, Atsushi-
dc.creatorColeman, Mathew L.-
dc.creatorKessler, Benedikt M.-
dc.creatorWappner, Pablo-
dc.creatorSchofield, Christopher J.-
dc.creatorRatcliffe, Peter J.-
dc.creatorCockman, Matthew E.-
dc.date2016-12-16T21:11:55Z-
dc.date2016-12-16T21:11:55Z-
dc.date2014-03-
dc.date2016-11-25T16:35:23Z-
dc.date.accessioned2019-04-29T15:55:36Z-
dc.date.available2019-04-29T15:55:36Z-
dc.identifierSingleton, Rachelle S.; Liu Yi, Febee; Formenti, Fabio; Ge, Wei; Sekirnik, Rok; et al.; OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation; National Academy Of Sciences; Proceedings Of The National Academy Of Sciences Of The United States Of America; 111; 11; 3-2014; 431-436-
dc.identifier0027-8424-
dc.identifierhttp://hdl.handle.net/11336/9653-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/305504-
dc.description2-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.-
dc.descriptionFil: Singleton, Rachelle S.. University of Oxford; Reino Unido-
dc.descriptionFil: Liu Yi, Febee. University of Oxford; Reino Unido. Pekin University; China-
dc.descriptionFil: Formenti, Fabio. University of Oxford; Reino Unido-
dc.descriptionFil: Ge, Wei. University of Oxford; Reino Unido-
dc.descriptionFil: Sekirnik, Rok. University of Oxford; Reino Unido-
dc.descriptionFil: Fischer, Roman. University of Oxford; Reino Unido-
dc.descriptionFil: Adam, Julie. University of Oxford; Reino Unido-
dc.descriptionFil: Pollard, Patrick J.. University of Oxford; Reino Unido-
dc.descriptionFil: Wolf, Alexander. University of Oxford; Reino Unido-
dc.descriptionFil: Thalhammer, Armin. University of Oxford; Reino Unido-
dc.descriptionFil: Loenarz, Christoph. University of Oxford; Reino Unido-
dc.descriptionFil: Flashman, Emily. University of Oxford; Reino Unido-
dc.descriptionFil: Yamamoto, Atsushi. University of Oxford; Reino Unido-
dc.descriptionFil: Coleman, Mathew L.. University of Oxford; Reino Unido-
dc.descriptionFil: Kessler, Benedikt M.. University of Oxford; Reino Unido-
dc.descriptionFil: Wappner, Pablo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina-
dc.descriptionFil: Schofield, Christopher J.. University of Oxford; Reino Unido-
dc.descriptionFil: Ratcliffe, Peter J.. University of Oxford; Reino Unido-
dc.descriptionFil: Cockman, Matthew E.. University of Oxford; Reino Unido-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherNational Academy Of Sciences-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://www.pnas.org/content/111/11/4031.long-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3964040/-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1073/pnas.1314482111-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.subjecttranslational control,-
dc.subjectribosome,-
dc.subject2-oxoglutarate oxygenase,-
dc.subjecthypoxia-
dc.subjectBioquímica y Biología Molecular-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleOGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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