Purified recombinant hARD1 does not catalyse acetylation of Lys532 of HIF-1alpha fragments in vitro.

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 Lett

journal_title

FEBS letters

authors

Murray-Rust TA,Oldham NJ,Hewitson KS,Schofield CJ

doi

10.1016/j.febslet.2006.02.012

keywords:

subject

Has Abstract

pub_date

2006-04-03 00:00:00

pages

1911-8

issue

8

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)00200-6

journal_volume

580

pub_type

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