Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1
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) d...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2015-08-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/07432 |
| _version_ | 1818018574996865024 |
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| author | Agata Butryn Jan M Schuller Gabriele Stoehr Petra Runge-Wollmann Friedrich Förster David T Auble Karl-Peter Hopfner |
| author_facet | Agata Butryn Jan M Schuller Gabriele Stoehr Petra Runge-Wollmann Friedrich Förster David T Auble Karl-Peter Hopfner |
| author_sort | Agata Butryn |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-14T07:41:29Z |
| format | Article |
| id | doaj.art-8a1f37505e6d4e819c117cb73e9351a2 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-14T07:41:29Z |
| publishDate | 2015-08-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-8a1f37505e6d4e819c117cb73e9351a22022-12-22T02:05:28ZengeLife Sciences Publications LtdeLife2050-084X2015-08-01410.7554/eLife.07432Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1Agata Butryn0Jan M Schuller1Gabriele Stoehr2Petra Runge-Wollmann3Friedrich Förster4David T Auble5Karl-Peter Hopfner6https://orcid.org/0000-0002-4528-8357Gene Center, Department of Biochemistry, Ludwig Maximilian University, Munich, GermanyDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, GermanyGene Center, Department of Biochemistry, Ludwig Maximilian University, Munich, GermanyGene Center, Department of Biochemistry, Ludwig Maximilian University, Munich, GermanyDepartment of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, GermanyDepartment of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, United StatesGene Center, Department of Biochemistry, Ludwig Maximilian University, Munich, Germany; Center for Integrated Protein Sciences, Munich, GermanySwi2/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.https://elifesciences.org/articles/07432Mot1NC2TBPtranscription regulationhybrid methodSwi2/Snf2 |
| spellingShingle | Agata Butryn Jan M Schuller Gabriele Stoehr Petra Runge-Wollmann Friedrich Förster David T Auble Karl-Peter Hopfner Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1 eLife Mot1 NC2 TBP transcription regulation hybrid method Swi2/Snf2 |
| title | Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1 |
| title_full | Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1 |
| title_fullStr | Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1 |
| title_full_unstemmed | Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1 |
| title_short | Structural basis for recognition and remodeling of the TBP:DNA:NC2 complex by Mot1 |
| title_sort | structural basis for recognition and remodeling of the tbp dna nc2 complex by mot1 |
| topic | Mot1 NC2 TBP transcription regulation hybrid method Swi2/Snf2 |
| url | https://elifesciences.org/articles/07432 |
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