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...
Main Authors: | Hannah Girstmair, Franziska Tippel, Abraham Lopez, Katarzyna Tych, Frank Stein, Per Haberkant, Philipp Werner Norbert Schmid, Dominic Helm, Matthias Rief, Michael Sattler, Johannes Buchner |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2019-08-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-019-11518-w |
Similar Items
-
A switch point in the molecular chaperone Hsp90 responding to client interaction
by: Daniel Andreas Rutz, et al.
Published: (2018-04-01) -
Hsp90 Co-chaperones Form Plastic Genetic Networks Adapted to Client Maturation
by: Maximilian M. Biebl, et al.
Published: (2020-08-01) -
Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery
by: Ting Li, et al.
Published: (2018-04-01) -
Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle
by: Maximilian M. Biebl, et al.
Published: (2021-02-01) -
Identification of degradation pathways for HSP90 client proteins
by: Li, Zhaobo
Published: (2017)