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  Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1.

Butryn, A., Schuller, J. M., Stoehr, G., Runge-Wollmann, P., Förster, F., Auble, D. T., et al. (2015). Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1. eLife, 4: e07432. doi:10.7554/eLife.07432.

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Butryn, Agata1, Author
Schuller, Jan M.2, Author              
Stoehr, Gabriele1, Author
Runge-Wollmann, Petra1, Author
Förster, Friedrich2, 3, Author              
Auble, David T1, Author
Hopfner, Karl-Peter1, Author
Affiliations:
1external, ou_persistent22              
2Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565148              
3Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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 Abstract: 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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Language(s): eng - English
 Dates: 2015
 Publication Status: Published online
 Pages: 22
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 26258880
DOI: 10.7554/eLife.07432
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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 4 Sequence Number: e07432 Start / End Page: - Identifier: Other: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X