Abstract:
:In humans, many responses to hypoxia including angiogenesis and erythropoiesis are mediated by the alpha/beta-heterodimeric transcription factor hypoxia inducible factor (HIF). The stability and/or activity of human HIF-1alpha are modulated by post-translational modifications including prolyl and asparaginyl hydroxylation, phosphorylation, and reportedly by acetylation of the side-chain of Lys532 by ARD1 (arrest defective protein 1 homologue), an acetyltransferase. Using purified recombinant human ARD1 (hARD1) we did not observe ARD1-mediated N-acetylation of Lys532 using fragments of HIF-1alpha. However, recombinant hARD1 from Escherichia coli was produced with partial N-terminal acetylation and was observed to undergo slow self-mediated N-terminal acetylation. The observations are consistent with the other data indicating that hARD1, at least alone, does not acetylate HIF-1alpha, and with reports on the N-terminal acetyltransferase activity of a recently reported heterodimeric complex comprising hARD1 and N-acetyltransferase protein.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Murray-Rust TA,Oldham NJ,Hewitson KS,Schofield CJdoi
10.1016/j.febslet.2006.02.012keywords:
subject
Has Abstractpub_date
2006-04-03 00:00:00pages
1911-8issue
8eissn
0014-5793issn
1873-3468pii
S0014-5793(06)00200-6journal_volume
580pub_type
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