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J Gen Virol 85 (2004), 2931-2935; DOI 10.1099/vir.0.80088-0

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© 2004 Society for General Microbiology

Short Communication

Feline foamy virus Tas protein is a DNA-binding transactivator

Shinya Omoto1, Ebiamadon Andi Brisibe2, Harumi Okuyama1 and Yoichi R. Fujii1

1 Molecular Biology and Retroviral Genetics Group, Division of Nutritional Sciences, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan
2 Research and Scientific Developments Division, Molecular Bio/Sciences Ltd, 124 MCC Road, Calabar, Cross River State, Nigeria

Correspondence
Yoichi R. Fujii
fatfuji{at}hotmail.com

Foamy viruses (FVs) harbour a transcriptional transactivator (Tas) and two Tas-responsive promoter regions, one in the 5' long terminal repeat (LTR) and the other an internal promoter (IP) in the envelope gene. To analyse the mechanism of transactivation of the FVs, the specificity of feline FV (FFV) Tas protein, which is more distantly related to the respective proteins of non-human primate origin, were investigated. FFV Tas has been shown specifically to activate gene expression from the cognate promoters. No cross-transactivation was noted of the prototype foamy virus and human immunodeficiency virus type 1 LTR. The putative transactivation response element of FFV Tas was mapped to the 5' LTR U3 region (approximately nt –228 to –195). FFV Tas binds to this element in addition to a previously described sequence (position –66 to –51). It is therefore concluded that FFV Tas is a DNA-binding transactivator that interacts with at least two regions in the virus LTR.




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S. Omoto and Y. R. Fujii
Regulation of human immunodeficiency virus 1 transcription by nef microRNA
J. Gen. Virol., March 1, 2005; 86(3): 751 - 755.
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