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dc.contributor.authorArnesen, Thomaseng
dc.contributor.authorBetts, Matthew J.eng
dc.contributor.authorPendino, Frédériceng
dc.contributor.authorLiberles, David A.eng
dc.contributor.authorAnderson, Daveeng
dc.contributor.authorCaro, Jaimeeng
dc.contributor.authorKong, Xianguoeng
dc.contributor.authorVarhaug, Jan Erikeng
dc.contributor.authorLillehaug, Johaneng
dc.description.abstract<p>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.</p> <p>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.</p> <p>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.</p>en
dc.format.extent1064704 byteseng
dc.publisherBioMed Centraleng
dc.rightsAttribution CC BYeng
dc.titleCharacterization of hARD2, a processed hARD1 gene duplicate, encoding a human protein N-α-acetyltransferaseeng
dc.typeJournal articleeng
dc.subject.nsiVDP::Matematikk og Naturvitenskap: 400::Basale biofag: 470::Molekylærbiologi: 473nob
dc.rights.holderCopyright 2006 Arnesen et al; licensee BioMed Central Ltd.
bora.peerreviewedPeer reviewedeng
bora.journalTitleBMC Biochemistryeng

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