• Corpus ID: 82213263

Regulatory elements that mediate transactivation by Tas in the internal promoter of bovine foamy virus.

@article{Li2000RegulatoryET,
  title={Regulatory elements that mediate transactivation by Tas in the internal promoter of bovine foamy virus.},
  author={Zhangcheng Li and Qiao Wentao and Liu Shuhong and Wang Jinzhong and Chen Qi-min and Geng Yunqi},
  journal={Chinese journal of virology},
  year={2000},
  volume={16},
  pages={232-237}
}
Lysine residues K 66 , K 109 , and K 110 in the bovine foamy virus transactivator protein are required for transactivation and viral replication
TLDR
Results indicate that lysine residues at positions 66, 109, and 110 in the BTas protein are crucial for BFV replication and suggest a potential role for BTas acetylation in regulating the viral life cycle.
Lysine residues K66, K109, and K110 in the bovine foamy virus transactivator protein are required for transactivation and viral replication
TLDR
Results indicate that lysine residues at positions 66, 109, and 110 in the BTas protein are crucial for BFV replication and suggest a potential role for BTas acetylation in regulating the viral life cycle.
Identi fi cation and functional characterization of BTas transactivator as a DNA-binding protein
a State Key Laboratory of Elemento-Organic Chemistry and Department of Chemical Biology, Nankai University, Tianjin 300071, China b Key Laboratory of Molecular Microbiology and Biotechnology
Subcellular localization analysis of bovine foamy virus Borf1 protein
TLDR
To analyze the subcellular localization of Borf1 during the BFV life cycle, this gene was cloned into a prokaryotic expression vector and expressed in a soluble form and western blot analysis showed that the antiserum could specifically recognize the Borf 1 protein that was expressed in 293T cells.
Guanine tetrad and palindromic sequence play critical roles in the RNA dimerization of bovine foamy virus
TLDR
It is found that two sites, designated SI and SII, within a 53-base RNA fragment, were essential for BFV dimerization in vitro, and suggest that dimerized might play a unique role in the BFV life cycle.