PXD016509 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | DnaK interaction and folding of firefly luciferase studied by hydrogen/deuterium exchange – mass spectrometry |
Description | The ATP-dependent chaperones of the Hsp70 class (DnaK in E. coli) function in protein folding in cooperation with J proteins and nucleotide exchange factors (DnaJ and GrpE in E. coli, respectively). Hsp70 prevents protein aggregation, increasing the folding yield, but whether it also enhances the rate of folding is unclear. Equilibrium hydrogen/deuterium exchange – mass spectrometry showed that DnaK stabilizes a poorly structured state of firefly luciferase (FLuc). Pulsed-label experiments, together with orthogonal analyses by spFRET, identified compact inter-domain misfolded states of FLuc that convert slowly to the native state. DnaK binding expands the misfolded region and thereby resolves the kinetically-trapped intermediates, with folding occurring upon GrpE-mediated release. By resolving misfolding and accelerating folding the Hsp70 system can maintain proteins in their native states under otherwise denaturing stress conditions. |
HostingRepository | PRIDE |
AnnounceDate | 2020-01-15 |
AnnouncementXML | Submission_2020-01-22_03:59:21.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | David Balchin |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; |
ModificationList | No PTMs are included in the dataset |
Instrument | Synapt MS |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-11-28 07:06:43 | ID requested | |
1 | 2020-01-15 00:44:05 | announced | |
⏵ 2 | 2020-01-22 03:59:22 | announced | 2020-01-22: Updated publication reference for PubMed record(s): 31953415. |
3 | 2020-02-17 03:18:36 | announced | 2020-01-22: Updated publication reference for PubMed record(s): 31953415.
2020-02-17: Updated publication reference for PubMed record(s): 31953415. |
Publication List
Imamoglu R, Balchin D, Hayer-Hartl M, Hartl FU, Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein. Nat Commun, 11(1):365(2020) [pubmed] |
Keyword List
curator keyword: Biological |
submitter keyword: dnak, folding, chaperone, firefly luciferase, deuterium exchange |
Contact List
F. Ulrich Hartl |
contact affiliation | Max Planck Institute of Biochemistry Department of Cellular Biochemistry Am Klopferspitz 18 82152 Martinsried, Germany |
contact email | uhartl@biochem.mpg.de |
lab head | |
David Balchin |
contact affiliation | Max Planck Institute of Biochemistry |
contact email | balchin@biochem.mpg.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD016509
- Label: PRIDE project
- Name: DnaK interaction and folding of firefly luciferase studied by hydrogen/deuterium exchange – mass spectrometry