Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6
SIRT6 plays essential roles in metabolism, tumor suppression, and DNA repair through the deacetylation of histone substrates. Here the authors use biophysical methods to investigate the molecular basis for SIRT6 interaction with the nucleosome core particle.
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2020-10-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-19018-y |
| _version_ | 1818890285471498240 |
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| author | Wallace H. Liu Jie Zheng Jessica L. Feldman Mark A. Klein Vyacheslav I. Kuznetsov Craig L. Peterson Patrick R. Griffin John M. Denu |
| author_facet | Wallace H. Liu Jie Zheng Jessica L. Feldman Mark A. Klein Vyacheslav I. Kuznetsov Craig L. Peterson Patrick R. Griffin John M. Denu |
| author_sort | Wallace H. Liu |
| collection | DOAJ |
| description | SIRT6 plays essential roles in metabolism, tumor suppression, and DNA repair through the deacetylation of histone substrates. Here the authors use biophysical methods to investigate the molecular basis for SIRT6 interaction with the nucleosome core particle. |
| first_indexed | 2024-12-19T17:22:29Z |
| format | Article |
| id | doaj.art-9e099b0632594eb7b9f5d6c425650d98 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-19T17:22:29Z |
| publishDate | 2020-10-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-9e099b0632594eb7b9f5d6c425650d982022-12-21T20:12:39ZengNature PortfolioNature Communications2041-17232020-10-0111111310.1038/s41467-020-19018-yMultivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6Wallace H. Liu0Jie Zheng1Jessica L. Feldman2Mark A. Klein3Vyacheslav I. Kuznetsov4Craig L. Peterson5Patrick R. Griffin6John M. Denu7Department of Biomolecular Chemistry, University of Wisconsin-MadisonDepartment of Molecular Medicine, Scripps Research FloridaProgram in Molecular Medicine, University of Massachusetts Medical SchoolDepartment of Biomolecular Chemistry, University of Wisconsin-MadisonDepartment of Biomolecular Chemistry, University of Wisconsin-MadisonProgram in Molecular Medicine, University of Massachusetts Medical SchoolDepartment of Molecular Medicine, Scripps Research FloridaDepartment of Biomolecular Chemistry, University of Wisconsin-MadisonSIRT6 plays essential roles in metabolism, tumor suppression, and DNA repair through the deacetylation of histone substrates. Here the authors use biophysical methods to investigate the molecular basis for SIRT6 interaction with the nucleosome core particle.https://doi.org/10.1038/s41467-020-19018-y |
| spellingShingle | Wallace H. Liu Jie Zheng Jessica L. Feldman Mark A. Klein Vyacheslav I. Kuznetsov Craig L. Peterson Patrick R. Griffin John M. Denu Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6 Nature Communications |
| title | Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6 |
| title_full | Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6 |
| title_fullStr | Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6 |
| title_full_unstemmed | Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6 |
| title_short | Multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by SIRT6 |
| title_sort | multivalent interactions drive nucleosome binding and efficient chromatin deacetylation by sirt6 |
| url | https://doi.org/10.1038/s41467-020-19018-y |
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