Asset Details
Do you wish to reserve the book?
Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
Do you wish to request the book?
Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein
2020
Overview
The ATP-dependent Hsp70 chaperones (DnaK in
E. coli
) mediate protein folding in cooperation with J proteins and nucleotide exchange factors (
E. coli
DnaJ and GrpE, respectively). The Hsp70 system prevents protein aggregation and increases folding yields. Whether it also enhances the rate of folding remains unclear. Here we show that DnaK/DnaJ/GrpE accelerate the folding of the multi-domain protein firefly luciferase (FLuc) ~20-fold over the rate of spontaneous folding measured in the absence of aggregation. Analysis by single-pair FRET and hydrogen/deuterium exchange identified inter-domain misfolding as the cause of slow folding. DnaK binding expands the misfolded region and thereby resolves the kinetically-trapped intermediates, with folding occurring upon GrpE-mediated release. In each round of release DnaK commits a fraction of FLuc to fast folding, circumventing misfolding. We suggest that by resolving misfolding and accelerating productive folding, the bacterial Hsp70 system can maintain proteins in their native states under otherwise denaturing stress conditions.
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 find that the bacterial Hsp70 actively promotes the folding of this multi-domain protein.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/33
/ 14/35
/ 82/80
/ 82/83
/ Animals
/ Bacteria
/ E coli
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - metabolism
/ Fluorescence resonance energy transfer
/ Folding
/ Heat-Shock Proteins - chemistry
/ Heat-Shock Proteins - metabolism
/ HSP40 Heat-Shock Proteins - chemistry
/ HSP40 Heat-Shock Proteins - metabolism
/ HSP70 Heat-Shock Proteins - chemistry
/ HSP70 Heat-Shock Proteins - metabolism
/ Humanities and Social Sciences
/ Kinetics
/ Luciferases, Firefly - chemistry
/ Luciferases, Firefly - genetics
/ Molecular Chaperones - metabolism
/ Proteins
/ Science
