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-Structure paper
タイトル | Cryo-EM reveals promoter DNA binding and conformational flexibility of the general transcription factor TFIID. |
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ジャーナル・号・ページ | Structure, Vol. 17, Issue 11, Page 1442-1452, Year 2009 |
掲載日 | 2009年11月11日 |
著者 | Hans Elmlund / Vera Baraznenok / Tomas Linder / Zsolt Szilagyi / Reza Rofougaran / Anders Hofer / Hans Hebert / Martin Lindahl / Claes M Gustafsson / |
PubMed 要旨 | The general transcription factor IID (TFIID) is required for initiation of RNA polymerase II-dependent transcription at many eukaryotic promoters. TFIID comprises the TATA-binding protein (TBP) and ...The general transcription factor IID (TFIID) is required for initiation of RNA polymerase II-dependent transcription at many eukaryotic promoters. TFIID comprises the TATA-binding protein (TBP) and several conserved TBP-associated factors (TAFs). Recognition of the core promoter by TFIID assists assembly of the preinitiation complex. Using cryo-electron microscopy in combination with methods for ab initio single-particle reconstruction and heterogeneity analysis, we have produced density maps of two conformational states of Schizosaccharomyces pombe TFIID, containing and lacking TBP. We report that TBP-binding is coupled to a massive histone-fold domain rearrangement. Moreover, docking of the TBP-TAF1(N-terminus) atomic structure to the TFIID map and reconstruction of a TAF-promoter DNA complex helps to account for TAF-dependent regulation of promoter-TBP and promoter-TAF interactions. |
リンク | Structure / PubMed:19913479 |
手法 | EM (単粒子) |
解像度 | 8.0 - 10.0 Å |
構造データ | EMDB-5134: EMDB-5135: |
由来 |
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