A methylated lysine is a switch point for conformational communication in the chaperone Hsp90
Methylation of a lysine residue in Hsp90 is a recently discovered post-translational modification but the mechanistic effects of this modification have remained unknown so far. Here the authors combine biochemical and biophysical approaches, molecular dynamics (MD) simulations and functional experim...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2020-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-15048-8 |
| _version_ | 1819129962697850880 |
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| author | Alexandra Rehn Jannis Lawatscheck Marie-Lena Jokisch Sophie L. Mader Qi Luo Franziska Tippel Birgit Blank Klaus Richter Kathrin Lang Ville R. I. Kaila Johannes Buchner |
| author_facet | Alexandra Rehn Jannis Lawatscheck Marie-Lena Jokisch Sophie L. Mader Qi Luo Franziska Tippel Birgit Blank Klaus Richter Kathrin Lang Ville R. I. Kaila Johannes Buchner |
| author_sort | Alexandra Rehn |
| collection | DOAJ |
| description | Methylation of a lysine residue in Hsp90 is a recently discovered post-translational modification but the mechanistic effects of this modification have remained unknown so far. Here the authors combine biochemical and biophysical approaches, molecular dynamics (MD) simulations and functional experiments with yeast and show that this lysine is a switch point, which specifically modulates conserved Hsp90 functions including co-chaperone regulation and client activation. |
| first_indexed | 2024-12-22T08:52:03Z |
| format | Article |
| id | doaj.art-e58f3663006545cf9df6166e474e1b1b |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-22T08:52:03Z |
| publishDate | 2020-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-e58f3663006545cf9df6166e474e1b1b2022-12-21T18:31:57ZengNature PortfolioNature Communications2041-17232020-03-0111111410.1038/s41467-020-15048-8A methylated lysine is a switch point for conformational communication in the chaperone Hsp90Alexandra Rehn0Jannis Lawatscheck1Marie-Lena Jokisch2Sophie L. Mader3Qi Luo4Franziska Tippel5Birgit Blank6Klaus Richter7Kathrin Lang8Ville R. I. Kaila9Johannes Buchner10Department 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 MünchenDepartment of Chemistry, Technische Universität MünchenDepartment of Chemistry, Technische Universität MünchenDepartment of Chemistry, Technische Universität MünchenMethylation of a lysine residue in Hsp90 is a recently discovered post-translational modification but the mechanistic effects of this modification have remained unknown so far. Here the authors combine biochemical and biophysical approaches, molecular dynamics (MD) simulations and functional experiments with yeast and show that this lysine is a switch point, which specifically modulates conserved Hsp90 functions including co-chaperone regulation and client activation.https://doi.org/10.1038/s41467-020-15048-8 |
| spellingShingle | Alexandra Rehn Jannis Lawatscheck Marie-Lena Jokisch Sophie L. Mader Qi Luo Franziska Tippel Birgit Blank Klaus Richter Kathrin Lang Ville R. I. Kaila Johannes Buchner A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 Nature Communications |
| title | A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
| title_full | A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
| title_fullStr | A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
| title_full_unstemmed | A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
| title_short | A methylated lysine is a switch point for conformational communication in the chaperone Hsp90 |
| title_sort | methylated lysine is a switch point for conformational communication in the chaperone hsp90 |
| url | https://doi.org/10.1038/s41467-020-15048-8 |
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