Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor.

Journal article

Factor-inhibiting hypoxia-inducible factor (FIH) catalyzes the β-hydroxylation of an asparagine residue in the C-terminal transcriptional activation domain of the hypoxia inducible factor (HIF), a modification that negatively regulates HIF transcriptional activity. FIH also catalyzes the hydroxylation of highly conserved Asn residues within the ubiquitous ankyrin repeat domain (ARD)-containing proteins. Hydroxylation has been shown to stabilize localized regions of the ARD fold in the case of...

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Authors: Yang, M; Ge, W; Chowdhury, R; Claridge, T; Kramer, H

• Publication status: Published
• Journal: Journal of biological chemistry
• Volume: 286
• Issue: 9
• Pages: 7648-7660
• Publication date: 2011-03-01
• DOI: 10.1074/jbc.m110.193540
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Signal Transduction; Catalytic Domain; Crystallography; Humans; Recombinant Proteins; Ankyrins; Peptide Fragments; Protein Structure, Tertiary; Protein Stability; Molecular Sequence Data; Asparagine; Aspartic Acid; Hydroxylation; Protein Processing, Post-Translational; HEK293 Cells; Mixed Function Oxygenases; Amino Acid Sequence; Cytoskeleton; Repressor Proteins