کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2050804 | 1074182 | 2006 | 8 صفحه PDF | دانلود رایگان |
In humans, many responses to hypoxia including angiogenesis and erythropoiesis are mediated by the α/β-heterodimeric transcription factor hypoxia inducible factor (HIF). The stability and/or activity of human HIF-1α 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-1α. 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-1α, and with reports on the N-terminal acetyltransferase activity of a recently reported heterodimeric complex comprising hARD1 and N-acetyltransferase protein.
Journal: FEBS Letters - Volume 580, Issue 8, 3 April 2006, Pages 1911–1918