title: The histone folds in transcription factor TFIID.
abstract: The transcription factor TFIID is a multimeric protein complex containing the TATA box-binding polypeptide (TBP) and TBP-associated factors. We have previously reported that the N-terminal regions of dTAFII62 and dTAFII42 have sequence similarities with histones H4 and H3. Here, we demonstrate that the histone-homologous regions of dTAFII62 and dTAFII42 form a heteromeric complex both in vitro and in a yeast two-hybrid system. Neither dTAFII62 nor dTAFII42 forms a homomeric complex, in agreement with a nucleosomal histone character. Moreover, circular dichroism measurements show that the heteromeric complex is dominated by alpha-helical secondary structure. These results strongly suggest the existence of a histone-like surface on TFIID.
authors.affiliation: Laboratory of Molecular Growth Regulation, NICHD, National Institutes of Health, Bethesda, Maryland 20892-2753, USA.
authors.forename: Y
authors.initials: Y
authors.lastname: Nakatani
authors.forename: S
authors.initials: S
authors.lastname: Bagby
authors.forename: M
authors.initials: M
authors.lastname: Ikura
mesh_terms: D001704:Biopolymers; D002942:Circular Dichroism; D006657:Histones / Q000737:chemistry*; D011401:Promoter Regions, Genetic; D017510:Protein Folding; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000737:chemistry*
chemical_list: D001704:Biopolymers; D006657:Histones; D035362:Transcription Factor TFIID; D014157:Transcription Factors