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-Structure paper
タイトル | Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1. |
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ジャーナル・号・ページ | Elife, Vol. 4, Year 2015 |
掲載日 | 2015年8月10日 |
![]() | Agata Butryn / Jan M Schuller / Gabriele Stoehr / Petra Runge-Wollmann / Friedrich Förster / David T Auble / Karl-Peter Hopfner / ![]() ![]() |
PubMed 要旨 | Swi2/Snf2 ATPases remodel substrates such as nucleosomes and transcription complexes to control a wide range of DNA-associated processes, but detailed structural information on the ATP-dependent ...Swi2/Snf2 ATPases remodel substrates such as nucleosomes and transcription complexes to control a wide range of DNA-associated processes, but detailed structural information on the ATP-dependent remodeling reactions is largely absent. The single subunit remodeler Mot1 (modifier of transcription 1) dissociates TATA box-binding protein (TBP):DNA complexes, offering a useful system to address the structural mechanisms of Swi2/Snf2 ATPases. Here, we report the crystal structure of the N-terminal domain of Mot1 in complex with TBP, DNA, and the transcription regulator negative cofactor 2 (NC2). Our data show that Mot1 reduces DNA:NC2 interactions and unbends DNA as compared to the TBP:DNA:NC2 state, suggesting that Mot1 primes TBP:NC2 displacement in an ATP-independent manner. Electron microscopy and cross-linking data suggest that the Swi2/Snf2 domain of Mot1 associates with the upstream DNA and the histone fold of NC2, thereby revealing parallels to some nucleosome remodelers. This study provides a structural framework for how a Swi2/Snf2 ATPase interacts with its substrate DNA:protein complex. |
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手法 | EM (単粒子) / X線回折 |
解像度 | 3.78 - 22.0 Å |
構造データ | ![]() EMDB-2828: ![]() PDB-4wzs: |
由来 |
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![]() | TRANSCRIPTION / protein-DNA complex / Swi2/Snf2 |