Duplicate divergence of two bacterial small heat shock proteins reduces the demand for Hsp70 in refolding of substrates.
Small heat shock proteins (sHsps) are a conserved class of ATP-independent chaperones that bind to aggregation-prone polypeptides at stress conditions. sHsps encage these polypeptides in assemblies, shielding them from further aggregation. To facilitate their subsequent solubilization and refolding...
Main Authors: | Igor Obuchowski, Artur Piróg, Milena Stolarska, Bartłomiej Tomiczek, Krzysztof Liberek |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2019-10-01
|
Series: | PLoS Genetics |
Online Access: | https://doi.org/10.1371/journal.pgen.1008479 |
Similar Items
-
Adenosine diphosphate restricts the protein remodeling activity of the Hsp104 chaperone to Hsp70 assisted disaggregation
by: Agnieszka Kłosowska, et al.
Published: (2016-05-01) -
Two-step mechanism of J-domain action in driving Hsp70 function.
by: Bartlomiej Tomiczek, et al.
Published: (2020-06-01) -
Evolution towards simplicity in bacterial small heat shock protein system
by: Piotr Karaś, et al.
Published: (2023-12-01) -
Structure and evolution of the 4-helix bundle domain of Zuotin, a J-domain protein co-chaperone of Hsp70.
by: Om Kumar Shrestha, et al.
Published: (2019-01-01) -
Heat Shock Protein 90 (Hsp90) and Hsp70 as Potential Therapeutic Targets in Autoimmune Skin Diseases
by: Stefan Tukaj, et al.
Published: (2022-08-01)