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Fig. 4 | Virology Journal

Fig. 4

From: Important role of N108 residue in binding of bovine foamy virus transactivator Tas to viral promoters

Fig. 4

Residue N108 is important for BTas transactivation. a Schematic representation of the BTas protein. BTas DNA binding domain (1–133 aa) and activation domain (198–249 aa) on the top are shown in the grey box. The dimerization domain (46–62 aa) is marked with a lighter grey box. Solid dots represent three lysines at positions 66, 109 and 110 which are also acetylated. Amino acids at position 108 are shown for BTas-Y and BTas-B. b HEK293T cells were transfected with BTas-Y, BTas-B, mutated BTas-B plasmids or empty vector (100 ng) together with 20 ng pBFV-LTR-Luc, 50 ng pEGFP-C3 and 10 ng pCMV-β-gal. Luciferase activity was measured 48 h post-transfection. Levels of BTas, GFP and tubulin proteins were measured by Western blotting. c-d pcDNA3.1(+), BTas-Y, BTas-B and BTas-B mutants were expressed in BFVL c and Cf2Th cells d. Luciferase activity was determined at 48 h post-transfection

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