Reactome | OGFOD1:Fe2+ hydroxylates a proline residue of RPS23

OGFOD1:Fe2+ hydroxylates a proline residue of RPS23

Stable Identifier

R-HSA-9630769

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

Synonyms

2-oxoglutarate + (ribosomal protein uS12)-L-proline + O2 => (ribosomal protein uS12)-(3S)-3-hydroxy-L-proline + CO2 + succinate

ReviewStatus

3/5

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OGFOD1:Fe2+ hydroxylates a proline residue of RPS23

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OGFOD1 (2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1) catalyzes the 3-hydroxylation of proline residue 62 of RPS23 (40S ribosomal protein S23) (Loenarz et al. 2014; Singleton et al. 2014). The active form of the enzyme is a monomer complexed with Fe2+ (Horita et al. 2015). Its nuclear localization is inferred from studies of the closely homologous Drosophila protein (Katz et al 2014).

Literature References

PubMed ID	Title	Journal	Year
24550463	Sudestada1, a Drosophila ribosomal prolyl-hydroxylase required for mRNA translation, cell homeostasis, and organ growth Liu-Yi, P, Sekirnik, R, Katz, MJ, Melani, M, Simonetta, S, Thomas, MG, Ge, W, Loenarz, C, Pérez-Pepe, M, Wappner, P, Thalhammer, A, Cockman, ME, Ratcliffe, PJ, Galagovsky, D, Schofield, CJ, Boccaccio, GL, Acevedo, JM	Proc. Natl. Acad. Sci. U.S.A.	2014
25728928	Structure of the ribosomal oxygenase OGFOD1 provides insights into the regio- and stereoselectivity of prolyl hydroxylases Aik, W, McDonough, MA, Thinnes, C, Scotti, JS, Thalhammer, A, Mottaghi-Taromsari, YS, Schofield, CJ, Ge, W, Horita, S, Loenarz, C	Structure	2015
24550462	Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy Sekirnik, R, McDonough, MA, Spivakovsky, E, Wolf, A, Kessler, BM, Thalhammer, A, Mackeen, MM, Cockman, ME, Ratcliffe, PJ, Schofield, CJ, Ge, W, Loenarz, C	Proc. Natl. Acad. Sci. U.S.A.	2014
24550447	OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in translation control and stress granule formation Liu-Yi, P, Sekirnik, R, Formenti, F, Wolf, A, Flashman, E, Coleman, ML, Fischer, R, Pollard, PJ, Ge, W, Loenarz, C, Wappner, P, Yamamoto, A, Adam, J, Kessler, BM, Thalhammer, A, Cockman, ME, Ratcliffe, PJ, Schofield, CJ, Singleton, RS	Proc. Natl. Acad. Sci. U.S.A.	2014