Gangloff, Y.G., Romier, C., Thuault, S., Werten, S., Davidson, I. (2001). The histone fold is a key structural motif of transcription factor TFIID. Trends Biochem. Sci. 26(4): 250--257.
FlyBase ID
FBrf0156064
Publication Type
Review
Abstract
Transcription factor TFIID is a multiprotein complex composed of the TATA binding protein and its associated factors, and is required for accurate and regulated initiation of transcription by RNA polymerase II. The subunit composition of this factor is highly conserved from yeast to mammals. X-ray crystallography and biochemical experiments have shown that the histone fold motif mediates many of the subunit interactions within this complex. These results, together with electron microscopy and yeast genetics, provide insights into the overall organization of this complex.
