TY - JOUR
T1 - Isolation and characterization of the Drosophila gene encoding the TATA box binding protein, TFIID
AU - Hoey, Timothy
AU - Dynlacht, Brian David
AU - Peterson, M. Gregory
AU - Pugh, B. Franklin
AU - Tjian, Robert
N1 - Funding Information:
8. D. Dynlacht and T. Hoey contributed equally to the work reported in this paper. We thank Jim Kadonaga for providing his TFIID fraction from1 Drosophila embryos, Laura Attardi for RNA samples, Larry Kau-var for the cDNA library, and Todd Laverty for performing the chromo- some in situ hybridiza:ions. We acknowledge Trevor Williams for pointing out the duplicated amino acid motif in the Drosophila and yeast TFIID proteins. We also thank Grace Gill, Richard Turner, and Steve Bell for their comments on the manuscript. This work was funded in part by a grant to R. T from the National Institutes of Health. T. H. is supported by an American Cancer Society postdoctoral fellowship, and M. G. P. and B. F. i? are funded by postdoctoral fellowships from the Leukemia Society of America.
PY - 1990/6/29
Y1 - 1990/6/29
N2 - To investigate the biochemical mechanisms involved in interactions between regulatory factors and the general transcription complex, we have cloned, expressed, and characterized the Drosophila gene encoding the TATA binding protein, dTFIID. Comparison of the protein sequences of the Drosophila and yeast TATA binding proteins reveals a bipartite organization consisting of a highly conserved, basic carboxy-terminal domain and a nonconserved amino-terminal region rich in Gln, Gly, Ser, and Met residues. Purified dTFIID protein binds specifically to the TATA sequence and activates basal-level transcription, and the conserved carboxy-terminal half of the molecule is sufficient for both activities. Partially purified TFIID from Drosophila cells mediates activation by the transcription factor Sp1. In contrast, purified dTFIID expressed from the cloned gene is unable to support Sp1-dependent activation, suggesting that other factors may be required to mediate interactions between upstream activators like Sp1 and the TATA binding protein.
AB - To investigate the biochemical mechanisms involved in interactions between regulatory factors and the general transcription complex, we have cloned, expressed, and characterized the Drosophila gene encoding the TATA binding protein, dTFIID. Comparison of the protein sequences of the Drosophila and yeast TATA binding proteins reveals a bipartite organization consisting of a highly conserved, basic carboxy-terminal domain and a nonconserved amino-terminal region rich in Gln, Gly, Ser, and Met residues. Purified dTFIID protein binds specifically to the TATA sequence and activates basal-level transcription, and the conserved carboxy-terminal half of the molecule is sufficient for both activities. Partially purified TFIID from Drosophila cells mediates activation by the transcription factor Sp1. In contrast, purified dTFIID expressed from the cloned gene is unable to support Sp1-dependent activation, suggesting that other factors may be required to mediate interactions between upstream activators like Sp1 and the TATA binding protein.
UR - https://www.scopus.com/pages/publications/0025358909
UR - https://www.scopus.com/pages/publications/0025358909#tab=citedBy
U2 - 10.1016/0092-8674(90)90682-5
DO - 10.1016/0092-8674(90)90682-5
M3 - Article
C2 - 2194666
AN - SCOPUS:0025358909
SN - 0092-8674
VL - 61
SP - 1179
EP - 1186
JO - Cell
JF - Cell
IS - 7
ER -