Structural similarity between TAFs and the heterotetrameric core of the histone octamer.
A complex of two TFIID TATA box-binding protein-associated factors (TA FIIs) is described at 2.0A resolution. The amino-terminal portions of dTAFII42 and dTAFII62 from Drosophila adopt the canonical histone fold, consisting of two short alpha-helices flanking a long central alpha-helix. Like histones H3 and H4, dTAFII42 and dTAFII62 form an ... intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAFII42/dTAFII62 complex exists as a heterotetramer, resembling the (H3/H4)2 heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.
Mesh Terms:
Amino Acid Sequence, Animals, Chickens, Crystallography, X-Ray, DNA-Binding Proteins, Drosophila, Drosophila Proteins, Escherichia coli, Histones, Models, Molecular, Molecular Sequence Data, Protein Conformation, RNA Polymerase II, Recombinant Proteins, Sequence Alignment, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Trans-Activators, Transcription Factor TFIID, Transcription Factors
Amino Acid Sequence, Animals, Chickens, Crystallography, X-Ray, DNA-Binding Proteins, Drosophila, Drosophila Proteins, Escherichia coli, Histones, Models, Molecular, Molecular Sequence Data, Protein Conformation, RNA Polymerase II, Recombinant Proteins, Sequence Alignment, TATA-Binding Protein Associated Factors, TATA-Box Binding Protein, Trans-Activators, Transcription Factor TFIID, Transcription Factors
Nature
Date: Mar. 28, 1996
PubMed ID: 8598927
View in: Pubmed Google Scholar
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