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...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
Materias:
Q
Acceso en línea:https://doaj.org/article/e58f3663006545cf9df6166e474e1b1b
Etiquetas: Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
id oai:doaj.org-article:e58f3663006545cf9df6166e474e1b1b
record_format dspace
spelling oai:doaj.org-article:e58f3663006545cf9df6166e474e1b1b2021-12-02T17:31:10ZA methylated lysine is a switch point for conformational communication in the chaperone Hsp9010.1038/s41467-020-15048-82041-1723https://doaj.org/article/e58f3663006545cf9df6166e474e1b1b2020-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15048-8https://doaj.org/toc/2041-1723Methylation 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.Alexandra RehnJannis LawatscheckMarie-Lena JokischSophie L. MaderQi LuoFranziska TippelBirgit BlankKlaus RichterKathrin LangVille R. I. KailaJohannes BuchnerNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
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.
format article
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
title 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_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_sort methylated lysine is a switch point for conformational communication in the chaperone hsp90
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/e58f3663006545cf9df6166e474e1b1b
work_keys_str_mv AT alexandrarehn amethylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT jannislawatscheck amethylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT marielenajokisch amethylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT sophielmader amethylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT qiluo amethylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT franziskatippel amethylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT birgitblank amethylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT klausrichter amethylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT kathrinlang amethylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT villerikaila amethylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT johannesbuchner amethylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT alexandrarehn methylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT jannislawatscheck methylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT marielenajokisch methylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT sophielmader methylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT qiluo methylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT franziskatippel methylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT birgitblank methylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT klausrichter methylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT kathrinlang methylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT villerikaila methylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
AT johannesbuchner methylatedlysineisaswitchpointforconformationalcommunicationinthechaperonehsp90
_version_ 1718380706527182848