Yeast TATA-binding protein TFIID binds to TATA elements with both consensus and nonconsensus DNA sequences.
AUTOR(ES)
Hahn, S
RESUMO
The DNA binding properties of the yeast TATA element-binding protein TFIID were investigated. The affinity (apparent equilibrium dissociation constant) of TFIID for the adenovirus major late promoter consensus TATA element is 2 x 10(-9) M, a value similar to the affinity of gene-specific regulatory proteins for their binding sites. TFIID binding is highly specific and recognizes nonspecific sites with approximately 10(5)-fold lower affinity. Despite this specificity, TFIID also binds with high affinity to several TATA elements that do not match the consensus TATA sequences (TATAAA and TATATA): the yeast LEU2 TATA (TATTATTTA), the simian virus 40 TATA (CTTATTTAT), and the yeast CYC1 -10 TATA (TTATACATT) all bound TFIID. Furthermore, TFIID was active in promoting transcription in vitro from the nonconsensus TATA elements. Thus, contrary to previous suggestions, the existence of nonconsensus TATA elements does not itself indicate the existence of multiple TATA-binding factors.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=297701Documentos Relacionados
- TFIIA Interacts with TFIID via Association with TATA-Binding Protein and TAF40
- Crystal structure of yeast TATA-binding protein and model for interaction with DNA.
- Wild-type p53 binds to the TATA-binding protein and represses transcription.
- A TATA-Binding Protein Mutant Defective for TFIID Complex Formation In Vivo
- Contribution of sequences downstream of the TATA element to a protein-DNA complex containing the TATA-binding protein.