|Title:||The Small Delta Antigen of Hepatitis Delta Virus Is an Acetylated Protein and Acetylation of Lysine 72 May Influence Its Cellular Localization and Viral Rna Synthesis||Authors:||MU, JUNG-JUNG
|Keywords:||HDV;HDAg;acetylation;p300;NLS||Issue Date:||2004||Journal Volume:||v.319||Journal Issue:||n.1||Start page/Pages:||60-70||Source:||VIROLOGY||Abstract:||
Hepatitis delta virus (HDV) is a single-stranded RNA virus that encodes two viral nucleocapsid proteins named small and large form hepatitis delta antigen (S-HDAg and L-HDAg). The S-HDAg is essential for viral RNA replication while the L- HDAg is required for viral assembly. In this study, we demonstrated that HDAg are acetylated proteins. Metabolic labeling with [H-3]acetate revealed that both forms of HDAg could be acetylated in vivo. The histone acetyltransferase ( HAT) domain of cellular acetyltransferase p300 could acetylate the full-length and the N- terminal 88 amino acids of S-HDAg in vitro. By mass spectrometric analysis of the modified protein, Lys-72 of S-HDAg was identified as one of the acetylation sites. Substitution of Lys-72 to Arg caused the mutant S-HDAg to redistribute from the nucleus to the cytoplasm. The mutant reduced viral RNA accumulation and resulted in the earlier appearance of L-HDAg. These results demonstrated that HDAg is an acetylated protein and mutation of HDAg at Lys-72 modulates HDAg subcellular localization and may participate in viral RNA nucleocytoplasmic shuttling and replication. (C) 2003 Elsevier Inc. All rights reserved
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