Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-α-acetyltransferase
1 Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway
2 Department of Surgical Sciences, Haukeland University Hospital, N-5021 Bergen, Norway
3 Computational Biology Unit, BCCS, University of Bergen, N-5020 Bergen, Norway
4 Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229, USA
5 Department of Medicine, Thomas Jefferson University, Philadelphia, PA19107, USA
BMC Biochemistry 2006, 7:13 doi:10.1186/1471-2091-7-13Published: 25 April 2006
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 ε-acetylation of histones and transcription factors. We recently described the human protein acetyltransferase hARD1 (
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-α-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-α-acetyltransferase is herein described. ARD2 potentially complements the functions of ARD1, adding more flexibility and complexity to protein N-α-acetylation in human cells as compared to lower organisms which only have one ARD.