Solution structure of the C-terminal core domain of human TFIIB: similarity to cyclin A and interaction with TATA-binding protein.
TFIIB is an essential component of the machinery that transcribes protein-coding genes. The three-dimensional structure of the human TFIIB core domain (TFIIBc) has been determined using multidimensional heteronuclear magnetic resonance spectroscopy. The molecule consists of two direct repeats that adopt similar alpha-helical folds, conferring pseudo-twofold symmetry. An extensive, central basic surface including an amphipathic alpha helix is critical to the function of TFIIB as a bridge between the TBP-promoter complex and RNA polymerase II and associated general and regulatory transcription factors. Similarities between the TFIIBc and cyclin A folds indicate that elements of the eukaryotic cell cycle control apparatus evolved from more fundamental transcriptional control components, demonstrating a link between the transcription and cell cycle molecular machineries.
Bagby
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Division of Molecular and Structural Biology Ontario Cancer Institute, Toronto, Canada.
Kim
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S
Maldonado
E
E
Tong
K I
KI
Reinberg
D
D
Ikura
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M
D000595:Amino Acid Sequence; D001665:Binding Sites / Q000235:genetics; D016213:Cyclins / Q000235:genetics*; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006801:Humans; D007091:Image Processing, Computer-Assisted; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D011401:Promoter Regions, Genetic / Q000235:genetics; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D016385:TATA Box / Q000235:genetics*; D035181:TATA-Box Binding Protein; D035581:Transcription Factor TFIIB; D014157:Transcription Factors / Q000235:genetics* / Q000378:metabolism* / Q000648:ultrastructure; D014158:Transcription, Genetic / Q000235:genetics
D016213:Cyclins; D004268:DNA-Binding Proteins; D035181:TATA-Box Binding Protein; D035581:Transcription Factor TFIIB; D014157:Transcription Factors; D004247:DNA