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Characterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-α-acetyltransferase
Arnesen, T ; Betts, MJ ; Pendino, F ; Liberles, DA ; Anderson, D ; Caro, J ; Kong, X ; Varhaug, JE ; Lillehaug, JR
Arnesen, T
Betts, MJ
Pendino, F
Liberles, DA
Anderson, D
Caro, J
Kong, X
Varhaug, JE
Lillehaug, JR
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Genre
Journal Article
Date
2006-04-25
Advisor
Committee member
Group
Department
Subject
Acetylation
Acetyltransferases
Amino Acid Sequence
Animals
Base Sequence
Cell Differentiation
Cell Line
Cell Line, Tumor
Chromosomes, Human, Pair 4
Cloning, Molecular
Enzyme Induction
Evolution, Molecular
Gene Duplication
Humans
Hypoxia-Inducible Factor 1, alpha Subunit
Macropodidae
Mice
Models, Molecular
Molecular Sequence Data
N-Terminal Acetyltransferase A
N-Terminal Acetyltransferase E
Phylogeny
Protein Conformation
Protein Processing, Post-Translational
RNA, Messenger
Rats
Retroelements
Sequence Alignment
Sequence Homology
Species Specificity
Tretinoin
Acetyltransferases
Amino Acid Sequence
Animals
Base Sequence
Cell Differentiation
Cell Line
Cell Line, Tumor
Chromosomes, Human, Pair 4
Cloning, Molecular
Enzyme Induction
Evolution, Molecular
Gene Duplication
Humans
Hypoxia-Inducible Factor 1, alpha Subunit
Macropodidae
Mice
Models, Molecular
Molecular Sequence Data
N-Terminal Acetyltransferase A
N-Terminal Acetyltransferase E
Phylogeny
Protein Conformation
Protein Processing, Post-Translational
RNA, Messenger
Rats
Retroelements
Sequence Alignment
Sequence Homology
Species Specificity
Tretinoin
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Journal Issue
DOI
10.1186/1471-2091-7-13
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. © 2006 Arnesen et al; licensee BioMed Central Ltd.
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Citation
Citation to related work
Springer Science and Business Media LLC
Has part
BMC Biochemistry
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