Nucleic Acids Research, Vol 25, Issue 2 379-387, Copyright © 1997 by Oxford University Press
DY Jin and KT Jeang
HTLV-I Tax protein is a potent transcriptional activator of viral and
cellular genes. Tax does not bind DNA directly but interacts through
protein-protein contact with host cell factors that recognize the viral
long terminal repeat (LTR). Domains within Tax needed for protein- protein
interaction have not been fully characterized. In studying transcriptional
function in yeast cells, we unexpectedly found that Tax functions optimally
not as a monomer, but as a homodimer. Here we have used the one hybrid and
two hybrid genetic approaches in yeast to investigate the region(s) within
Tax necessary for self-association. Dimer formation was also confirmed
biochemically by using electrophoretic mobility shift (EMSA) and supershift
assays. Twenty two Tax point mutants were utilized to map relevant
residues. Genetic results from this series of mutants revealed that a
necessary region for dimerization is contained within a previously
characterized zinc finger domain. Two loss-of-function Tax mutants, each
poorly active when assayed individually, were found to have complementing
activity when co-expressed together. This genetic complementation suggests
a mechanism fortrans-activation resulting from simultaneous but non-
identical contact with a responsive target by each of two Tax monomers in a
dimer.
ARTICLES
HTLV-I Tax self-association in optimal trans-activation function
Molecular Virology Section, Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892-0460, USA.
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