IN higher eukaryotes the RNA polymerase II transcription factor TFIID
is composed of a TATA-box-binding protein (TBP) and a set of tightly b
ound polypeptides, designated TBP-associated fao tors (TAF(II)s). One
or more TAF(II)s are coactivators that are required for activated but
not basal transcription(1-3). The eukaryotic transcription machinery i
s highly conserved and it is therefore puzzling that TAF(II)s have aot
been identified in yeast. Here we use TBP as a protein-affinity ligan
d to isolate from yeast a multi-subunit complex that is required speci
fically for activated transcription by RNA polymerase II. Microsequenc
e analysis and cloning of two subunits of this complex reveal that the
y are the homologues of known mammalian and Drosophila TAF(II)s. The g
enes encoding these two yeast TAF(II)s are essential, suggesting that
activated transcription is required for viability of Saccharomyces cer
evisiae.