Bergen Open Research Archive >
Faculty of Mathematics and Natural Sciences >
Department of Molecular Biology >
Department of Molecular Biology (Various) >
Please use this identifier to cite or link to this item:
http://hdl.handle.net/1956/1911
|
| Title: | Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-α-acetyltransferase |
| Authors: | Arnesen, Thomas
Betts, Matthew J.
Pendino, Frédéric
Liberles, David A.
Anderson, Dave
Caro, Jaime
Kong, Xianguo
Varhaug, Jan E.
Lillehaug, Johan R. |
| Issue Date: | 25-Apr-2006 |
| Publisher: | BioMed Central |
| Series/Report no.: | BMC Biochemistry 7(13) |
| 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 (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. |
| URI: | http://dx.doi.org/10.1186/1471-2091-7-13
http://hdl.handle.net/1956/1911 |
| Appears in Collections: | Department of Molecular Biology (Various)
|
Items in BORA are protected by copyright, with all rights reserved, unless otherwise indicated.
