2004
DOI: 10.1128/jvi.78.23.13325-13334.2004
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Hepatitis Delta Virus Antigen Is Methylated at Arginine Residues, and Methylation Regulates Subcellular Localization and RNA Replication

Abstract: Hepatitis delta virus (HDV) contains a circular RNA which encodes a single protein, hepatitis delta antigen (HDAg). HDAg exists in two forms, a small form (S-HDAg) and a large form (L-HDAg). S-HDAg can transactivate HDV RNA replication. Recent studies have shown that posttranslational modifications, such as phosphorylation and acetylation, of S-HDAg can modulate HDV RNA replication. Here we show that S-HDAg can be methylated by protein arginine methyltransferase (PRMT1) in vitro and in vivo. The major methylat… Show more

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Cited by 84 publications
(69 citation statements)
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References 57 publications
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“…Genomic RNA synthesis (from the antigenomic template) is sensitive to a low concentration of ␣-amanitin (1 g/ml), whereas the antigenomic RNA synthesis (from the genomic template) is surprisingly resistant to a very high concentration (100 g/ml) of the drug (by comparison, the transcription of the 0.8-kb mRNA is also sensitive to the low concentration of ␣-amanitin) (40,43,47). The genomic RNA synthesis requires an S-HDAg that is phosphorylated and methylated, whereas the antigenomic RNA synthesis can be mediated by an unmethylated S-HDAg (34,49,60). Certain phosphorylation-defective mutants (S177A) and methylationdefective mutants (R13A) of HDAg can mediate the antigenomic RNA synthesis but not the genomic RNA synthesis.…”
Section: Replication Of Genomic Versus Antigenomic Rnamentioning
confidence: 99%
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“…Genomic RNA synthesis (from the antigenomic template) is sensitive to a low concentration of ␣-amanitin (1 g/ml), whereas the antigenomic RNA synthesis (from the genomic template) is surprisingly resistant to a very high concentration (100 g/ml) of the drug (by comparison, the transcription of the 0.8-kb mRNA is also sensitive to the low concentration of ␣-amanitin) (40,43,47). The genomic RNA synthesis requires an S-HDAg that is phosphorylated and methylated, whereas the antigenomic RNA synthesis can be mediated by an unmethylated S-HDAg (34,49,60). Certain phosphorylation-defective mutants (S177A) and methylationdefective mutants (R13A) of HDAg can mediate the antigenomic RNA synthesis but not the genomic RNA synthesis.…”
Section: Replication Of Genomic Versus Antigenomic Rnamentioning
confidence: 99%
“…Methylation of Arg-13, acetylation of Lys-72, and phosphorylation of Ser-177 and Ser-123 have been reported to affect the subcellular localization of HDAg and RNA replication (26,34,50,65). Most of these modifications are important for the functions of S-HDAg in HDV RNA replication.…”
Section: Structure Of Hdv Rna and Hdagmentioning
confidence: 99%
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“…As such, some amino acid residues in S-and L-HDAg appear to be critical for posttranslational modifications [1,10] . Of these residues Arg-13, Lys-72 and Ser-177 in S-HDAg undergo methylation [18] , acetylation [19] and phosphorylation [20] , respectively [1,10] . There are also multiple lysin residues throughout the whole S-HDAg as well as 66 amino acids at the N-terminal part of this protein which act as sumoylation sites of the protein.…”
Section: Protein Modifications Of Hdvmentioning
confidence: 99%