Yeast TATA-binding protein

Adams, C.A., Kar, S.R., Hopper, J.E., and Fried, M.G. (2004) Self-association of the amino-terminal domain of the yeast TATA-binding protein./. Biol. Chem. 279, 1376-1382. 

D.I. Chasman, K.M. Flaherty, P.A. Sharp and R.D. Komberg. Crystal structure of yeast TATA-binding protein and model for interaction with DNA. Proc. Natl. Acad. Sci. USA 90 (1993) 8174-8. 

G.M. Perez-Howard, P.A. Weil and J.M. Beechem. Yeast TATA binding protein interaction with DNA fluorescence determination of oligomeric state, equilibrium binding, on-rate, and dissociation kinetics. Biochemistry 34 (1995) 8005-17. 

K.M. Arndt, C.R. Wobbe, H.S. Ricupero, K. Struhl and F. Winston. Equivalent mutations in the two repeats of yeast TATA-binding protein confer distinct TATA recognition specificities. Mol. Cell. Biol. 14 (1994) 3719-28. 

D. Poon, et al. Genetic and biochemical analyses of yeast TATA-binding protein mutants. J Biol Chem 268 (1993) 5(X)5-13. 

FIGURE 11.20 Model of yeast TATA-binding protein (TBP) binding to DNA. The DNA... 

Ohdate, H., Lim, C.R., Kokubo, T., Matsubara, K.I., Kimata, Y., and Kohno, K. (2003) Impairment of the DNA-binding activity of the TATA-binding protein (TBP) renders the transcriptional function of Rvb2p/Tih2p, the yeast RuvB-like protein, essential for cell growth. J. Biol. Chem. 278, 14647-14656. 

B.P. Cormack and K. Struhl. The TATA-binding protein is required for transcription by all three nuclear RNA polymerases in yeast cells. Cell 69 (1992) 685-96. 

C.R. Wobbe and K. Struhl. Yeast and human TATA-binding proteins have nearly identical DNA sequence requirements for transcription in vitro. Mol. Cell. Biol. 10 (1990) 3859-67. 

Deprez, E., Arrebola, R., Conesa, C., and Sentenac, A. (1999). A subunit of yeast TFIIIC participates in the recruitment of TATA-binding protein. Mol. Cell. Biol. 19, 8042-8051. 

Ghavidel, A., and Schultz, M. C. (1997). Casein kinase II regulation of yeast TFIIIB is mediated by the TATA-binding protein. Genes Dev. 11, 2780-2789. 

Kassavetis, G. A., Joazeiro, C. A., Pisano, M., Geiduschek, E. P., Colbert, T., Hahn, S., and Blanco, J. A. (1992). The role of the TATA-binding protein in the assembly and function of the multisubunit yeast RNA polymerase III transcription factor, TFIIIB. Cell 71, 1055-1064. 

Figure 9.3 Comparison of the consensus nucleotide sequence of the TATA box (a) and the sequences of the DNA fragments used in the crystal structure determinations of the TATA box-binding proteins from yeast (b) and the plant Arabidopsis thaliana (c).

Fig. 1.16. Bending of DNA in the TATA box. The DNA is kinked in the complex of the TATA box binding protein (yeast) with the 8 base pair TATA box (Kim et al., 1993). The DNA is deformed in the region near the kink the minor groove, which faces the protein, is clearly widened. Molscript drawing (Kraulis, 1991).

Proteins of the yeast SWFSNF family can initiate a modification of nucleosome structure to enable the interaction of the transcription factors with the nucleosome-bound DNA. Proteins of this class can function as anti-repressors by opposing the general repression of chromatin structure. The SWl/SNF proteins are contained in a large protein complex. They can modify nucleosome structure under ATP hydrolysis in such a way as to strengthen the binding of transcription factors, such as GAL4 or the TATA box binding protein, to nucleosome-bound DNA (Cote et al., 1994,). 

The crystal structure of a human TATA-box-binding protein (hTBP), complexed with TATA-box DNA, may be compared with that of a yeast TBP/TATA-box complex and a similar isoform of TBP firom Arabidopsis thaliana, bound to a TATA box in an adenoviral p>romoter (Plate 19).25-27... 

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