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Thuault S Gangloff YG Kirchner J Sanders S Werten S Romier C Weil PA Davidson I 《The Journal of biological chemistry》2002,277(47):45510-45517
Yeast TFIID comprises the TATA binding protein and 14 TBP-associated factors (TAF(II)s), nine of which contain histone-fold domains (HFDs). The C-terminal region of the TFIID-specific yTAF4 (yTAF(II)48) containing the HFD shares strong sequence similarity with Drosophila (d)TAF4 (dTAF(II)110) and human TAF4 (hTAF(II)135). A structure/function analysis of yTAF4 demonstrates that the HFD, a short conserved C-terminal domain (CCTD), and the region separating them are all required for yTAF4 function. Temperature-sensitive mutations in the yTAF4 HFD alpha2 helix or the CCTD can be suppressed upon overexpression of yTAF12 (yTAF(II)68). Moreover, coexpression in Escherichia coli indicates direct yTAF4-yTAF12 heterodimerization optimally requires both the yTAF4 HFD and CCTD. The x-ray crystal structure of the orthologous hTAF4-hTAF12 histone-like heterodimer indicates that the alpha3 region within the predicted TAF4 HFD is unstructured and does not correspond to the bona fide alpha3 helix. Our functional and biochemical analysis of yTAF4, rather provides strong evidence that the HFD alpha3 helix of the TAF4 family lies within the CCTD. These results reveal an unexpected and novel HFD organization in which the alpha3 helix is separated from the alpha2 helix by an extended loop containing a conserved functional domain. 相似文献
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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 下载免费PDF全文
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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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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