The basal transcription factor TFIID plays a central role in the regulation of gene expression in Eukaryota and is a large protein complex composed of TATA box-binding protein (TBP) and 14 kinds of TBP-associated factors (TAF). TFIID directly recognizes and binds to different kinds of core promoter elements that localize near the transcription initiation site and forms a scaffold for the other basal transcription factors to assemble. At the same time, it transmits transcriptional activation signal originating from transcription regulating factors to RNA polymerase II. Taf6p is one of the subunits of TFIID and in the case of budding yeast, it is composed of 516 amino acid residues. Taf6p is also a subunit of histoneacetylase complex SAGA which is said to have an overlapping function with TFIID. The protein contains histone folds in its interior and forms TAF octamer together with Taf4p, Taf9p and Taf12p.
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