The amino-terminal tails of the core histones and the translational position of the TATA box determine TBP/TFIIA association with nucleosomal DNA

• Published in: Nucleic acids research 1995-11, Vol.23 (22), p.4557-4564
• Main Authors: Godde, James S., Nakatani, Yoshibiro, Wolffe, Alan P.
• Format: Article
• Language: English
• Subjects: Animals; Base Sequence; Binding Sites; DNA, Ribosomal - chemistry; DNA, Ribosomal - genetics; DNA, Ribosomal - metabolism; DNA-Binding Proteins - metabolism; Histones - chemistry; Histones - metabolism; Models, Structural; Molecular Sequence Data; Nucleic Acid Conformation; Nucleosomes - metabolism; Protein Biosynthesis; Protein Conformation; RNA, Ribosomal, 5S - genetics; TATA Box; TATA-Box Binding Protein; Transcription Factor TFIIA; Transcription Factors - metabolism; Xenopus
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/23.22.4557

We establish that the TATA binding protein (TBP) in the presence of TFIIA recognizes the TATA box in nucleosomal DNA dependent on the dissociation of the amino-terminal tails of the core histones from the nucleosome and the position of the TATA box within the nucleosome. We examine TBP/TFIIA access to the TATA box with this sequence placed in four distinct rotational frames with reference to the histone surface and at three distinct translational positions at the edge, side and dyad axis of the nucleosome. Under our experimental conditions, we find that the preferential translational position at which TBP/TFIIA can bind the TATA box is within linker DNA at the edge of the nucleosome and that binding is facilitated if contacts made by the amino-terminal tails of the histones with nucleosomal DNA are eliminated. TBP/TFIIA binding to DNA at the edge of the nucleosome occurs with the TATA box in all four rotational positions. This is indicative of TBP/TFIIA association directing the dissociation of the TATA box from the surface of the histone octamer.