Transcriptional RegulationTranscription of genes is tightly regulated by a large number of proteins. TFIID plays a central role in recognition of the TATA box and subsequent recruitment of other factors such as TFIIB. Both TFIID and TFIIB are the targets of transcriptional activators and suppressors, which also contribute to the efficiency of gene transcription. We have solved the structure of TFIIBc (1TFB) in collaboration with Dr. D. Reinberg. In 1998, we determined the solution structure of TATA binding protein (TBP) in complex with the N-terminal suppressor domain of TBP-associated factor 230 or TAF230 (1TBA), which revealed an elegant mechanism for autoinhibition involving molecular mimicry of the partially unwound structure of a TBP-bound TATA element (Liu et al., 1998).
Liu, D., Ishima, R., Tong, K.I., Bagby, S., Kokubo, T., Muhandiram, D.R., Kay, L.E., Nakatani, Y., and Ikura, M. (1998) Solution Structure of a TBP-TAFII230 Complex: Protein Mimicry of the minor Groove Surface of the TATA Box Unwound by TBP. Cell 94, 573-583.
Bagby, S., Kim, S., Maldonado, E., Tong, K.I., Reinberg, D. and Ikura, M. (1995) The Solution Structure of the Carboxy-terminal Core Domain of Human TFIIB: Similarity to Cyclin A and Interaction with the TATA Binding Protein. Cell 82, 857-867.