EUKARYOTIC transcriptional activators may stimulate RNA polymerase II
activity by promoting assembly of preinitiation complexes on promoters
through their interactions with one or more components of the basal m
achinery(1,2). On the basis of its central role in initiating transcri
ption-complex formation upon binding to the TATA box, the general tran
scription factor TFIID, which includes the TATA-binding protein (TBP)
and several TBP-associated factors(3-5), has been implicated as a targ
et for activators. Consistent with this idea, an increasing number of
activators have been reported to bind directly to TBP6-9. To assess th
e functional importance of these in vitro interactions for transcripti
onal regulation in vivo, we made use of a novel strategy in yeast to s
how that a physical interaction with TBP is sufficient for a sequence-
specific DNA-binding protein to increase initiation of transcription b
y RNA polymerase II. These results imply that binding of TFIID to prom
oter elements is a limiting step in transcription complex assembly in
vivo.