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Purified recombinant hARD1 does not catalyse acetylation of Lys 532 of HIF‐1α fragments in vitro
Author(s) -
Murray-Rust Thomas A.,
Oldham Neil J.,
Hewitson Kirsty S.,
Schofield Christopher J.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.02.012
Subject(s) - acetylation , acetyltransferase , recombinant dna , hypoxia inducible factors , biochemistry , chemistry , microbiology and biotechnology , cleavage (geology) , in vitro , hydroxylation , phosphorylation , p300 cbp transcription factors , biology , enzyme , gene , paleontology , fracture (geology) , histone acetyltransferases
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 Lys 532 by ARD1 (arrest defective protein 1 homologue), an acetyltransferase. Using purified recombinant human ARD1 (hARD1) we did not observe ARD1‐mediated N ‐acetylation of Lys 532 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.