Document Type
Article
Publication Date
1-1-2006
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 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. 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-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. CONCLUSION: 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.
Recommended Citation
Arnesen, Thomas; Betts, Matthew J; Pendino, Frédéric; Liberles, David A; Anderson, Dave; Caro, Jaime; Kong, Xianguo; Varhaug, Jan E; and Lillehaug, Johan R, "Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-alpha-acetyltransferase." (2006). Department of Medicine Faculty Papers. Paper 43.
https://jdc.jefferson.edu/medfp/43
PubMed ID
16638120
Comments
This article has been peer reviewed and is published in BMC Biochemistry Volume 7, 25 April 2006, Article number 13. The published version is available at DOI: 10.1186/1471-2091-7-13. Copyright © BioMed Central Ltd.