Transcription initiation factor TFIIB recruits RNA polymerase II to th
e promoter subsequent to interaction with a preformed TFIID-promoter c
omplex. The domains of TFIIB required for binding to the TFIID-promote
r complex and for transcription initiation have been determined. The c
arboxyl-terminal two-thirds of TFIIB, which contains two direct repeat
s and two basic residue repeats, is sufficient for interaction with th
e TFIID-promoter complex. An extra 84-residue amino-terminal region, w
ith no obvious known structural motifs, is required for basal transcri
ption activity. Basic residues within the second basic repeat of TFIIB
are necessary for stable interaction with the TFIID-promoter complex,
whereas the basic character of the first basic repeat is not. Functio
nal roles of other potential structural motifs are discussed in light
of the present study.