Taxi of human T-cell leukemia virus type 1 (HTLV-1) is an enigmatic vi
ral transactivator that regulates expression of the viral gene and als
o several cellular genes normally controlled by various mitogenic sign
als. However, previous studies have failed to define the functional do
mains of Taxi for enhancer specificities and for transcriptional activ
ation (95% of the protein portion was indispensable for the activation
function). This complexity has hampered understanding of the molecula
r basis of Taxi action. In this study, we analysed the activation func
tion of a Taxi fused to the heterologous DNA-binding domain of the yea
st transcription factor GAL4 and dissected the domain required for the
activation function by using derivatives of a Taxi mutant with an ins
ertion between amino acids (a.a.) 170 and 171. Analysis of the derivat
ives of the mutant fusion protein having various partial overlaps enco
mpassing the interrupted site suggested that two contiguous stretches,
AD-I (2-255 a.a.) and AD-II (227-337 a.a.), should be both intact for
the activation function of Taxi and that they form a functional activ
ation domain.