Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-α-acetyltransferase
Amino Acid Sequence
Cell Line, Tumor
Chromosomes, Human, Pair 4
Hypoxia-Inducible Factor 1, alpha Subunit
Molecular Sequence Data
N-Terminal Acetyltransferase A
N-Terminal Acetyltransferase E
Protein Processing, Post-Translational
Permanent link to this recordhttp://hdl.handle.net/20.500.12613/5636
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AbstractBackground: 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 (human Arrest Defective 1). hARD1 interacts with NATH (N-Acetyl Transferase Human) 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. © 2006 Arnesen et al; licensee BioMed Central Ltd.
Citation to related workSpringer Science and Business Media LLC
Has partBMC Biochemistry
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