PXD043837-2

PXD043837 is an original dataset announced via ProteomeXchange.

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	2023-09-07
AnnouncementXML	Submission_2023-09-07_02:26:05.465.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	JorgeCuéllar
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive; LTQ Orbitrap

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.

submitter keyword: DNAJA2 structure,chaperone, Hsp70 system, J-domain proteins, protein folding

JorgeCuellar
contact affiliation	Department of Macromolecular Structure, National Centre for Biotechnology (CNB-CSIC), 28049 Madrid, Spain.
contact email	jcuellar@cnb.csic.es
lab head
JorgeCuéllar
contact affiliation	CNB-CSIC
contact email	jcuellar@cnb.csic.es
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD043837
     1. Label: PRIDE project
     2. Name: The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70