Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle
p23 is a co-chaperone of Hsp90 but its mode of action is mechanistically not well understood. Here, the authors combine in vitro and yeast in vivo assays, biochemical measurements and NMR experiments to characterize p23 and identify two conserved helical elements in the intrinsically disordered C-te...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2021-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-21063-0 |
| _version_ | 1818681924879646720 |
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| author | Maximilian M. Biebl Abraham Lopez Alexandra Rehn Lee Freiburger Jannis Lawatscheck Birgit Blank Michael Sattler Johannes Buchner |
| author_facet | Maximilian M. Biebl Abraham Lopez Alexandra Rehn Lee Freiburger Jannis Lawatscheck Birgit Blank Michael Sattler Johannes Buchner |
| author_sort | Maximilian M. Biebl |
| collection | DOAJ |
| description | p23 is a co-chaperone of Hsp90 but its mode of action is mechanistically not well understood. Here, the authors combine in vitro and yeast in vivo assays, biochemical measurements and NMR experiments to characterize p23 and identify two conserved helical elements in the intrinsically disordered C-terminal tail of p23 that together with the folded domain of p23 regulate the Hsp90 ATPase activity and affect the binding and maturation of Hsp90 clients. |
| first_indexed | 2024-12-17T10:10:41Z |
| format | Article |
| id | doaj.art-a9b045045e0840e9b855e22c23e4ac09 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-17T10:10:41Z |
| publishDate | 2021-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-a9b045045e0840e9b855e22c23e4ac092022-12-21T21:53:02ZengNature PortfolioNature Communications2041-17232021-02-0112111310.1038/s41467-021-21063-0Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycleMaximilian M. Biebl0Abraham Lopez1Alexandra Rehn2Lee Freiburger3Jannis Lawatscheck4Birgit Blank5Michael Sattler6Johannes Buchner7Department of Chemistry, Technische Universität MünchenDepartment of Chemistry, Technische Universität MünchenDepartment of Chemistry, Technische Universität MünchenDepartment of Chemistry, Technische Universität MünchenDepartment of Chemistry, Technische Universität MünchenDepartment of Chemistry, Technische Universität MünchenDepartment of Chemistry, Technische Universität MünchenDepartment of Chemistry, Technische Universität Münchenp23 is a co-chaperone of Hsp90 but its mode of action is mechanistically not well understood. Here, the authors combine in vitro and yeast in vivo assays, biochemical measurements and NMR experiments to characterize p23 and identify two conserved helical elements in the intrinsically disordered C-terminal tail of p23 that together with the folded domain of p23 regulate the Hsp90 ATPase activity and affect the binding and maturation of Hsp90 clients.https://doi.org/10.1038/s41467-021-21063-0 |
| spellingShingle | Maximilian M. Biebl Abraham Lopez Alexandra Rehn Lee Freiburger Jannis Lawatscheck Birgit Blank Michael Sattler Johannes Buchner Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle Nature Communications |
| title | Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle |
| title_full | Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle |
| title_fullStr | Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle |
| title_full_unstemmed | Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle |
| title_short | Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle |
| title_sort | structural elements in the flexible tail of the co chaperone p23 coordinate client binding and progression of the hsp90 chaperone cycle |
| url | https://doi.org/10.1038/s41467-021-21063-0 |
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