Email updates

Keep up to date with the latest news and content from BMC Biochemistry and BioMed Central.

Open Access Highly Accessed Research article

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

Thomas Arnesen12*, Matthew J Betts3, Frédéric Pendino1, David A Liberles3, Dave Anderson4, Jaime Caro5, Xianguo Kong5, Jan E Varhaug2 and Johan R Lillehaug1

Author Affiliations

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

For all author emails, please log on.

BMC Biochemistry 2006, 7:13  doi:10.1186/1471-2091-7-13

Published: 25 April 2006

Abstract

Background

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 (

    h
uman
    Ar
rest
    D
efective
    1
). hARD1 interacts with NATH (
    N
-
    A
cetyl
    T
ransferase
    H
uman) forming a complex expressing protein N-terminal α-acetylation activity.

Results

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.

Conclusion

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.