title: The histone fold is a key structural motif of transcription factor TFIID.
abstract: Transcription factor TFIID is a multiprotein complex composed of the TATA binding protein and its associated factors, and is required for accurate and regulated initiation of transcription by RNA polymerase II. The subunit composition of this factor is highly conserved from yeast to mammals. X-ray crystallography and biochemical experiments have shown that the histone fold motif mediates many of the subunit interactions within this complex. These results, together with electron microscopy and yeast genetics, provide insights into the overall organization of this complex.
authors: Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP, BP 163 67404, Illkirch Cédex, C.U. de, Strasbourg, France.
authors: Y G
authors: YG
authors: Gangloff
authors: C
authors: C
authors: Romier
authors: S
authors: S
authors: Thuault
authors: S
authors: S
authors: Werten
authors: I
authors: I
authors: Davidson
mesh_terms: D000595:Amino Acid Sequence; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017386:Sequence Homology, Amino Acid; D035362:Transcription Factor TFIID; D019473:Transcription Factors, TFII / Q000737:chemistry / Q000378:metabolism*
chemical_list: D006657:Histones; D035362:Transcription Factor TFIID; D019473:Transcription Factors, TFII