Nucleic Acids Research, Vol 24, Issue 12 2324-2330, Copyright © 1996 by Oxford University Press
R Gupta, A Emili, G Pan, H Xiao, M Shales, J Greenblatt and CJ Ingles
Contact between a transcriptional activator and one or more components of
the RNA polymerase II transcription initiation machinery is generally
believed important for activators to function. Several different molecular
targets have been suggested for direct contact by herpes simplex virus
virion protein VP16, including the general initiation factor TFIIB. In this
report we have used several strategies to critically assess this
interaction between VP16 and TFIIB. Affinity columns of VP16 bound TFIIB
activity from HeLa cell extracts and the binding was reduced by mutations
in the activation domain of VP16. In assays of direct binding, VP16 bound
recombinant human TFIIB but not Drosophila or yeast TFIIB. Unlike binding
from an extract, however, we found that the interaction between VP16 and
recombinant human TFIIB was not affected by mutations in VP16 that reduce
transactivation. Point mutations within human TFIIB that reduce
transactivation by VP16 have been shown to reduce VP16 binding, but we show
here that these same mutations critically affect both the important
TBP-TFIIB interaction and the ability of TFIIB to support
activator-independent basal transcription in vitro. Taken together our
results suggest more evidence is needed to support the notion that TFIIB is
a functionally important target for the activator VP16.
ARTICLES
Characterization of the interaction between the acidic activation domain of VP16 and the RNA polymerase II initiation factor TFIIB
Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada.
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