Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state
Swi2/Snf2 ATPases remodel protein:DNA complexes in all of the fundamental chromosome-associated processes. The single-subunit remodeler Mot1 dissociates TATA box-binding protein (TBP):DNA complexes and provides a simple model for obtaining structural insights into the action of Swi2/Snf2 ATPases. Pr...
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| Format: | Article |
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eLife Sciences Publications Ltd
2018-10-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/37774 |
| _version_ | 1818028536110252032 |
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| author | Agata Butryn Stephan Woike Savera J Shetty David T Auble Karl-Peter Hopfner |
| author_facet | Agata Butryn Stephan Woike Savera J Shetty David T Auble Karl-Peter Hopfner |
| author_sort | Agata Butryn |
| collection | DOAJ |
| description | Swi2/Snf2 ATPases remodel protein:DNA complexes in all of the fundamental chromosome-associated processes. The single-subunit remodeler Mot1 dissociates TATA box-binding protein (TBP):DNA complexes and provides a simple model for obtaining structural insights into the action of Swi2/Snf2 ATPases. Previously we reported how the N-terminal domain of Mot1 binds TBP, NC2 and DNA, but the location of the C-terminal ATPase domain remained unclear (Butryn et al., 2015). Here, we report the crystal structure of the near full-length Mot1 from Chaetomium thermophilum. Our data show that Mot1 adopts a ring like structure with a catalytically inactive resting state of the ATPase. Biochemical analysis suggests that TBP binding switches Mot1 into an ATP hydrolysis-competent conformation. Combined with our previous results, these data significantly improve the structural model for the complete Mot1:TBP:DNA complex and suggest a general mechanism for Mot1 action. |
| first_indexed | 2024-12-10T05:05:21Z |
| format | Article |
| id | doaj.art-a9d37a6313fb41d2aa07dbfd62a188d2 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-12-10T05:05:21Z |
| publishDate | 2018-10-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-a9d37a6313fb41d2aa07dbfd62a188d22022-12-22T02:01:17ZengeLife Sciences Publications LtdeLife2050-084X2018-10-01710.7554/eLife.37774Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting stateAgata Butryn0https://orcid.org/0000-0002-5227-4770Stephan Woike1Savera J Shetty2David T Auble3Karl-Peter Hopfner4https://orcid.org/0000-0002-4528-8357Department of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, GermanyDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, GermanyDepartment of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, United StatesDepartment of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, United StatesDepartment of Biochemistry, Ludwig-Maximilians-Universität München, Munich, Germany; Gene Center, Ludwig-Maximilians-Universität München, Munich, Germany; Center for Integrated Protein Sciences Munich, Munich, GermanySwi2/Snf2 ATPases remodel protein:DNA complexes in all of the fundamental chromosome-associated processes. The single-subunit remodeler Mot1 dissociates TATA box-binding protein (TBP):DNA complexes and provides a simple model for obtaining structural insights into the action of Swi2/Snf2 ATPases. Previously we reported how the N-terminal domain of Mot1 binds TBP, NC2 and DNA, but the location of the C-terminal ATPase domain remained unclear (Butryn et al., 2015). Here, we report the crystal structure of the near full-length Mot1 from Chaetomium thermophilum. Our data show that Mot1 adopts a ring like structure with a catalytically inactive resting state of the ATPase. Biochemical analysis suggests that TBP binding switches Mot1 into an ATP hydrolysis-competent conformation. Combined with our previous results, these data significantly improve the structural model for the complete Mot1:TBP:DNA complex and suggest a general mechanism for Mot1 action.https://elifesciences.org/articles/37774Chaetomium thermophilumX-ray crystallographytranscription regulationSwi2/Snf2 remodeler |
| spellingShingle | Agata Butryn Stephan Woike Savera J Shetty David T Auble Karl-Peter Hopfner Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state eLife Chaetomium thermophilum X-ray crystallography transcription regulation Swi2/Snf2 remodeler |
| title | Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state |
| title_full | Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state |
| title_fullStr | Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state |
| title_full_unstemmed | Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state |
| title_short | Crystal structure of the full Swi2/Snf2 remodeler Mot1 in the resting state |
| title_sort | crystal structure of the full swi2 snf2 remodeler mot1 in the resting state |
| topic | Chaetomium thermophilum X-ray crystallography transcription regulation Swi2/Snf2 remodeler |
| url | https://elifesciences.org/articles/37774 |
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