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The TFIID Components Human TAFII140 and Drosophila BIP2 (TAFII155) Are Novel Metazoan Homologues of Yeast TAFII47 Containing a Histone Fold and a PHD Finger
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Yann-Gaël Gangloff Jean-Christophe Pointud Sylvie Thuault Lucie Carr Christophe Romier Selen Muratoglu Marjorie Brand Laszlo Tora Jean-Louis Couderc Irwin Davidson 《Molecular and cellular biology》2001,21(15):5109-5121
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Petros Papadopoulos Laura Gutiérrez Jeroen Demmers Elisabeth Scheer Farzin Pourfarzad Dimitris N. Papageorgiou Elena Karkoulia John Strouboulis Harmen J. G. van de Werken Reinier van der Linden Peter Vandenberghe Dick H. W. Dekkers Sjaak Philipsen Frank Grosveld Làszlò Tora 《Molecular and cellular biology》2015,35(12):2103-2118
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Werten S Mitschler A Romier C Gangloff YG Thuault S Davidson I Moras D 《The Journal of biological chemistry》2002,277(47):45502-45509
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Shao H Revach M Moshonov S Tzuman Y Gazit K Albeck S Unger T Dikstein R 《Molecular and cellular biology》2005,25(1):206-219
A major function of TFIID is core promoter recognition. TFIID consists of TATA-binding protein (TBP) and 14 TBP-associated factors (TAFs). Most of them contain a histone fold domain (HFD) that lacks the DNA-contacting residues of histones. Whether and how TAF HFDs contribute to core promoter DNA binding are yet unresolved. Here we examined the DNA binding activity of TAF9, TAF6, TAF4b, and TAF12, which are related to histones H3, H4, H2A, and H2B, respectively. Each of these TAFs has intrinsic DNA binding activity adjacent to or within the HFD. The DNA binding domains were mapped to evolutionarily conserved and essential regions. Remarkably, HFD-mediated interaction enhanced the DNA binding activity of each of the TAF6-TAF9 and TAF4b-TAF12 pairs and of a histone-like octamer complex composed of the four TAFs. Furthermore, HFD-mediated interaction stimulated sequence-specific binding by TAF6 and TAF9. These results suggest that TAF HFDs merge with other conserved domains for efficient and specific core promoter binding. 相似文献