PXD016509

PXD016509 is an original dataset announced via ProteomeXchange.

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_2020-02-17_03:18:34.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

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.

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]

curator keyword: Biological

submitter keyword: dnak, folding, chaperone, firefly luciferase, deuterium exchange

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

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2020/01/PXD016509

PRIDE project URI

• PRIDE
  1. PXD016509
     1. Label: PRIDE project
     2. Name: DnaK interaction and folding of firefly luciferase studied by hydrogen/deuterium exchange – mass spectrometry