Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
The Hsp70 system prevents protein aggregation and increases folding yields, but it is unknown whether it also enhances the rate of folding. Here the authors combine refolding assays, FRET and hydrogen/deuterium exchange-mass spectrometry measurements to study the folding of firefly luciferase and fi...
Guardado en:
Autores principales: | Rahmi Imamoglu, David Balchin, Manajit Hayer-Hartl, F. Ulrich Hartl |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2020
|
Materias: | |
Acceso en línea: | https://doaj.org/article/6125957e2a10438cac86795beb9c3d88 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
The HSP70 co-chaperone DNAJC14 targets misfolded pendrin for unconventional protein secretion
por: Jinsei Jung, et al.
Publicado: (2016) -
LONP1 and mtHSP70 cooperate to promote mitochondrial protein folding
por: Chun-Shik Shin, et al.
Publicado: (2021) -
HSP70-Hrd1 axis precludes the oncorepressor potential of N-terminal misfolded Blimp-1s in lymphoma cells
por: Wen-Fang Wang, et al.
Publicado: (2017) -
The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation
por: Kaushik Bhattacharya, et al.
Publicado: (2020) -
Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor
por: Bahareh Eftekharzadeh, et al.
Publicado: (2019)