PXD043837 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70 |
Description | J-domain proteins tune the specificity of Hsp70s, engaging them in precise functions. Despite their essential role, the structure and function of many J-domain proteins remain largely unknown. We explore human DNAJA2, a class A J-domain protein, finding that it reversibly oligomerises into highly-ordered, tubular structures that can be dissociated by Hsc70, the constitutively expressed Hsp70 isoform. Cryoelectron microscopy and mutational studies reveal that multivalent interactions between different domains are involved in self-association. Oligomer dissociation into dimers potentiates its interaction with unfolded client proteins. Closely spaced J domains in the tubular structure could allow transfer of several Hsc70 molecules to cooperatively remodel the unfolded substrate, explaining the efficient recovery of DNAJA2-bound clients. The disordered C-terminal domain, comprising the last 52 residues, regulates its holding activity and productive interaction with Hsc70. These in vitro findings suggest that the association equilibrium of DNAJA2 could regulate its interaction with client proteins and Hsc70. |
HostingRepository | PRIDE |
AnnounceDate | 2023-11-14 |
AnnouncementXML | Submission_2023-11-14_07:19:27.327.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Jorge Cuéllar |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | No PTMs are included in the dataset |
Instrument | Q Exactive; LTQ Orbitrap |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-07-17 04:01:14 | ID requested | |
1 | 2023-09-05 15:10:38 | announced | |
2 | 2023-09-07 02:26:05 | announced | 2023-09-07: Updated project metadata. |
⏵ 3 | 2023-11-14 07:19:27 | announced | 2023-11-14: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: DNAJA2 structure,chaperone, Hsp70 system, J-domain proteins, protein folding |
Contact List
Jorge Cuellar |
contact affiliation | Department of Macromolecular Structure, National Centre for Biotechnology (CNB-CSIC), 28049 Madrid, Spain. |
contact email | jcuellar@cnb.csic.es |
lab head | |
Jorge Cuéllar |
contact affiliation | CNB-CSIC |
contact email | jcuellar@cnb.csic.es |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD043837
- Label: PRIDE project
- Name: The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70