Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing.
Science
; 325(5936): 90-3, 2009 Jul 03.
Article
en En
| MEDLINE
| ID: mdl-19574390
The finding that the metazoan hypoxic response is regulated by oxygen-dependent posttranslational hydroxylations, which regulate the activity and lifetime of hypoxia-inducible factor (HIF), has raised the question of whether other hydroxylases are involved in the regulation of gene expression. We reveal that the splicing factor U2 small nuclear ribonucleoprotein auxiliary factor 65-kilodalton subunit (U2AF65) undergoes posttranslational lysyl-5-hydroxylation catalyzed by the Fe(II) and 2-oxoglutarate-dependent dioxygenase Jumonji domain-6 protein (Jmjd6). Jmjd6 is a nuclear protein that has an important role in vertebrate development and is a human homolog of the HIF asparaginyl-hydroxylase. Jmjd6 is shown to change alternative RNA splicing of some, but not all, of the endogenous and reporter genes, supporting a specific role for Jmjd6 in the regulation of RNA splicing.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Ribonucleoproteínas
/
Proteínas Nucleares
/
Empalme Alternativo
/
Receptores de Superficie Celular
Tipo de estudio:
Risk_factors_studies
Límite:
Humans
Idioma:
En
Revista:
Science
Año:
2009
Tipo del documento:
Article
Pais de publicación:
Estados Unidos