TFIID binds in the minor groove of the TATA box.
We have analyzed the interaction of the general RNA polymerase II transcription factor TFIID with its DNA-binding site, the TATA box (consensus sequence TATAAAA). We have demonstrated that TFIID, unlike most sequence-specific DNA-binding proteins, interacts primarily within the minor groove of the DNA helix. This was established by a novel approach involving complete replacement of the thymines and adenines in the TATA box with cytosines and inosines, respectively. This substitution exchanged the major groove of TATAAAA for that of the sequence CGCGGGG, without altering the surface of the minor groove. The unusual DNA-binding properties of TFIID revealed by this study have important implications for TFIID specificity and function and, more generally, for sequence-specific recognition by DNA-binding proteins.
Starr
D B
DB
Department of Chemistry, University of Oregon, Eugene 97403.
Hawley
D K
DK
D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000378:metabolism* / Q000648:ultrastructure; D004268:DNA-Binding Proteins / Q000378:metabolism*; D005609:Free Radicals / Q000737:chemistry; D006878:Hydroxides / Q000737:chemistry; D008745:Methylation; D008969:Molecular Sequence Data; D009841:Oligonucleotides / Q000737:chemistry / Q000378:metabolism; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism; D012045:Regulatory Sequences, Nucleic Acid; D012441:Saccharomyces cerevisiae; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000378:metabolism*
D004268:DNA-Binding Proteins; D005609:Free Radicals; D006878:Hydroxides; D009841:Oligonucleotides; D011994:Recombinant Proteins; D035362:Transcription Factor TFIID; D014157:Transcription Factors; D004247:DNA