Artículo
The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases
Markolovic, Suzana; Zhuang, Qinqin; Wilkins, Sarah E.; Eaton, Charlotte D.; Abboud, Martine I.; Katz, Maximiliano Javier
; McNeil, Helen E.; Leśniak, Robert K.; Hall, Charlotte; Struwe, Weston B.; Konietzny, Rebecca; Davis, Simon; Yang, Ming; Ge, Wei; Benesch, Justin L. P.; Kessler, Benedikt M.; Ratcliffe, Peter J.; Cockman, Matthew E.; Fischer, Roman; Wappner, Pablo
; Chowdhury, Rasheduzzaman; Coleman, Mathew L.; Schofield, Christopher J.
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Fecha de publicación:
07/2018
Editorial:
Nature Publishing Group
Revista:
Nature Chemical Biology
ISSN:
1552-4450
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
Biochemical, structural and cellular studies reveal Jumonji-C (JmjC) domain-containing 7 (JMJD7) to be a 2-oxoglutarate (2OG)-dependent oxygenase that catalyzes (3S)-lysyl hydroxylation. Crystallographic analyses reveal JMJD7 to be more closely related to the JmjC hydroxylases than to the JmjC demethylases. Biophysical and mutation studies show that JMJD7 has a unique dimerization mode, with interactions between monomers involving both N- and C-terminal regions and disulfide bond formation. A proteomic approach identifies two related members of the translation factor (TRAFAC) family of GTPases, developmentally regulated GTP-binding proteins 1 and 2 (DRG1/2), as activity-dependent JMJD7 interactors. Mass spectrometric analyses demonstrate that JMJD7 catalyzes Fe(ii)- and 2OG-dependent hydroxylation of a highly conserved lysine residue in DRG1/2; amino-acid analyses reveal that JMJD7 catalyzes (3S)-lysyl hydroxylation. The functional assignment of JMJD7 will enable future studies to define the role of DRG hydroxylation in cell growth and disease.
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Articulos(IIBBA)
Articulos de INST.DE INVEST.BIOQUIMICAS DE BS.AS(I)
Articulos de INST.DE INVEST.BIOQUIMICAS DE BS.AS(I)
Citación
Markolovic, Suzana; Zhuang, Qinqin; Wilkins, Sarah E.; Eaton, Charlotte D.; Abboud, Martine I.; et al.; The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases; Nature Publishing Group; Nature Chemical Biology; 14; 7; 7-2018; 688-695
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