Human TAFII28 and TAFII18 Interact through a Histone Fold Encoded by Atypical Evolutionary Conserved Motifs Also Found in the SPT3 Family

作者: Catherine Birck , Olivier Poch , Christophe Romier , Marc Ruff , Gabrielle Mengus

DOI: 10.1016/S0092-8674(00)81423-3

关键词:

摘要: Abstract Determination of the crystal structure human TBP-associated factor (hTAF II )28/hTAF 18 heterodimer shows that these TAF s form a novel histone-like pair in TFIID complex. The histone folds hTAF 28 and were not predicted from their primary sequence, indicating define family atypical fold sequences. motifs are also present N- C-terminal regions SPT3 proteins, suggesting may be reconstituted by intramolecular rather than classical intermolecular interactions. existence additional pairs both SAGA complexes is more commonly used motif for mediating TAF–TAF interactions previously believed.

参考文章(50)
M. May, G. Mengus, A. C. Lavigne, P. Chambon, I. Davidson, Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors. The EMBO Journal. ,vol. 15, pp. 3093- 3104 ,(1996) , 10.1002/J.1460-2075.1996.TB00672.X
Alexander Hoffmann, Cheng-Ming Chiang, Thomas Oelgeschläger, Xiaoling Xie, Stephen K. Burley, Yoshihiro Nakatani, Robert G. Roeder, A histone octamer-like structure within TFIID Nature. ,vol. 380, pp. 356- 359 ,(1996) , 10.1038/380356A0
Song Tan, Yvonne Hunziker, David F. Sargent, Timothy J. Richmond, Crystal structure of a yeast TFIIA/TBP/DNA complex. Nature. ,vol. 381, pp. 127- 134 ,(1996) , 10.1038/381127A0
G. Arents, E. N. Moudrianakis, The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 92, pp. 11170- 11174 ,(1995) , 10.1073/PNAS.92.24.11170