The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range
S. cerevisiae encodes two Hsp90 isoforms, the constitutively expressed Hsc82 and stress-inducible Hsp82 that are 97% identical. Here, the authors combine a range of biophysical methods and show that they differ in their enzymatic properties, resilience to stress and client range, which suggests that...
Guardado en:
Autores principales: | Hannah Girstmair, Franziska Tippel, Abraham Lopez, Katarzyna Tych, Frank Stein, Per Haberkant, Philipp Werner Norbert Schmid, Dominic Helm, Matthias Rief, Michael Sattler, Johannes Buchner |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/99faff43afb1456f9d5206c5879c275f |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
A switch point in the molecular chaperone Hsp90 responding to client interaction
por: Daniel Andreas Rutz, et al.
Publicado: (2018) -
A methylated lysine is a switch point for conformational communication in the chaperone Hsp90
por: Alexandra Rehn, et al.
Publicado: (2020) -
The Hsp90 machinery facilitates the transport of diphtheria toxin into human cells
por: Manuel Schuster, et al.
Publicado: (2017) -
Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90
por: Sophie L. Mader, et al.
Publicado: (2020) -
Structure-guided design of an Hsp90β N-terminal isoform-selective inhibitor
por: Anuj Khandelwal, et al.
Publicado: (2018)