FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor.
Genes Dev
; 16(12): 1466-71, 2002 Jun 15.
Article
em En
| MEDLINE
| ID: mdl-12080085
ABSTRACT
Mammalian cells adapt to hypoxic conditions through a transcriptional response pathway mediated by the hypoxia-inducible factor, HIF. HIF transcriptional activity is suppressed under normoxic conditions by hydroxylation of an asparagine residue within its C-terminal transactivation domain, blocking association with coactivators. Here we show that the protein FIH-1, previously shown to interact with HIF, is an asparaginyl hydroxylase. Like known hydroxylase enzymes, FIH-1 is an Fe(II)-dependent enzyme that uses molecular O(2) to modify its substrate. Together with the recently discovered prolyl hydroxylases that regulate HIF stability, this class of oxygen-dependent enzymes comprises critical regulatory components of the hypoxic response pathway.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Asparagina
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Proteínas Repressoras
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Transcrição Gênica
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Oxigenases de Função Mista
Idioma:
En
Ano de publicação:
2002
Tipo de documento:
Article