Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-α-acetyltransferase

Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway.
BMC Biochemistry (Impact Factor: 1.44). 02/2006; 7(1):13. DOI: 10.1186/1471-2091-7-13
Source: PubMed


Protein acetylation is increasingly recognized as an important mechanism regulating a variety of cellular functions. Several human protein acetyltransferases have been characterized, most of them catalyzing epsilon-acetylation of histones and transcription factors. We recently described the human protein acetyltransferase hARD1 (human Arrest Defective 1). hARD1 interacts with NATH (N-Acetyl Transferase Human) forming a complex expressing protein N-terminal alpha-acetylation activity.
We here describe a human protein, hARD2, with 81 % sequence identity to hARD1. The gene encoding hARD2 most likely originates from a eutherian mammal specific retrotransposition event. hARD2 mRNA and protein are expressed in several human cell lines. Immunoprecipitation experiments show that hARD2 protein potentially interacts with NATH, suggesting that hARD2-NATH complexes may be responsible for protein N-alpha-acetylation in human cells. In NB4 cells undergoing retinoic acid mediated differentiation, the level of endogenous hARD1 and NATH protein decreases while the level of hARD2 protein is stable.
A human protein N-alpha-acetyltransferase is herein described. ARD2 potentially complements the functions of ARD1, adding more flexibility and complexity to protein N-alpha-acetylation in human cells as compared to lower organisms which only have one ARD.

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Available from: Thomas Arnesen, Aug 14, 2015
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    • "NATH (N-acetyl transferase human) is involved in protein acetylation which represents an important post-translational modification regulating oncogenesis, apoptosis and cell cycle. NATH resulted to be over-expressed at the mRNA level in papillary thyroid carcinomas compared to non-neoplastic thyroid tissue [8]. "
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