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Vol. 16, No. 12, pp. 1466-1471, June 15, 2002
1 Department of Molecular BioSciences (Biochemistry) and
the Centre for the Molecular Genetics of Development, Adelaide
University SA 5005, Australia; 2 CSIRO Health Sciences and
Nutrition, Parkville VIC 3052, Australia; 3 Department of
Biochemistry, University of Texas Southwestern Medical Center,
Dallas, Texas 75390-9152, USA
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 O2 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.
[Key Words: Asparaginyl hydroxylase; hypoxia; oxygen sensing; HIF]
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