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.
Xie
X
X
Laboratory of Molecular Biophysics, The Rockefeller University, New York, 10021, USA.
Kokubo
T
T
Cohen
S L
SL
Mirza
U A
UA
Hoffmann
A
A
Chait
B T
BT
Roeder
R G
RG
Nakatani
Y
Y
Burley
S K
SK
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D018360:Crystallography, X-Ray; D004268:DNA-Binding Proteins / Q000737:chemistry; D004330:Drosophila; D029721:Drosophila Proteins; D004926:Escherichia coli; D006657:Histones / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012319:RNA Polymerase II / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D016415:Sequence Alignment; D035381:TATA-Binding Protein Associated Factors; D035181:TATA-Box Binding Protein; D015534:Trans-Activators / Q000737:chemistry*; D035362:Transcription Factor TFIID; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism
D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; D006657:Histones; D011994:Recombinant Proteins; D035381:TATA-Binding Protein Associated Factors; D035181:TATA-Box Binding Protein; C084976:Taf6 protein, Drosophila; D015534:Trans-Activators; D035362:Transcription Factor TFIID; D014157:Transcription Factors; C084120:e(y)1 protein, Drosophila; D012319:RNA Polymerase II