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Lysine acetylation sites in bovine foamy virus transactivator BTas are important for its DNA binding activity
- Source :
- Virology. (1):21-26
- Publisher :
- Elsevier Inc.
-
Abstract
- Cellular acetylation signaling is important for viral gene regulation, particularly during the transactivation of retroviruses. The regulatory protein of bovine foamy virus (BFV), BTas, is a transactivator that augments viral gene transcription from both the long terminal repeat (LTR) promoter and the internal promoter (IP). In this study, we report that the histone acetyltransferase (HAT), p300, specifically acetylates BTas both in vivo and in vitro. Further studies demonstrated that BTas acetylation markedly enhances its transactivation activity. Mutagenesis analysis identified three lysines at positions 66, 109 and 110 in BTas that are acetylated by p300. The K110R mutant lost its binding to BFV promoter as well as its ability to activate BFV promoter. The acetylation of K66 and K109 may contribute to increased BTas binding ability. These results suggest that the p300-acetylated lysines of BTas are important for transactivation of BFV promoters and therefore have an important role in BFV replication.
- Subjects :
- DNA Mutational Analysis
p300
P300-CBP Transcription Factors
Cell Line
Bovine foamy virus
Transactivation
Viral Proteins
Transcription (biology)
Virology
Cricetinae
Animals
Humans
p300-CBP Transcription Factors
Regulation of gene expression
biology
Lysine
Promoter
Acetylation
Histone acetyltransferase
DNA
Molecular biology
Long terminal repeat
Amino Acid Substitution
Host-Pathogen Interactions
biology.protein
Mutagenesis, Site-Directed
Trans-Activators
Spumavirus
BTas
Protein Binding
Subjects
Details
- Language :
- English
- ISSN :
- 00426822
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Virology
- Accession number :
- edsair.doi.dedup.....0ddc544de43c410a8221af806a44bd86
- Full Text :
- https://doi.org/10.1016/j.virol.2011.07.003