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PXD043837

PXD043837 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70
DescriptionJ-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.
HostingRepositoryPRIDE
AnnounceDate2023-11-14
AnnouncementXMLSubmission_2023-11-14_07:19:27.327.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterJorge Cuéllar
SpeciesList scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationListNo PTMs are included in the dataset
InstrumentQ Exactive; LTQ Orbitrap
Dataset History
RevisionDatetimeStatusChangeLog Entry
02023-07-17 04:01:14ID requested
12023-09-05 15:10:38announced
22023-09-07 02:26:05announced2023-09-07: Updated project metadata.
32023-11-14 07:19:27announced2023-11-14: 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 affiliationDepartment of Macromolecular Structure, National Centre for Biotechnology (CNB-CSIC), 28049 Madrid, Spain.
contact emailjcuellar@cnb.csic.es
lab head
Jorge Cuéllar
contact affiliationCNB-CSIC
contact emailjcuellar@cnb.csic.es
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
Repository Record List
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