PXD020268-3

PXD020268 is an original dataset announced via ProteomeXchange.

Title	DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network
Description	From biosynthesis to assembly into nucleosomes, histones are handed through a cascade of histone chaperones, which shield histones from non-specific interactions. Whether mechanisms exist to safeguard the histone fold during histone chaperone handover events or to release trapped intermediates is unclear. Using structure-guided and functional proteomics, we identify and characterize a histone chaperone function of DNAJC9, a heat shock co-chaperone that promotes HSP70-mediated catalysis. We elucidate the structure of DNAJC9, in a histone H3-H4 co-chaperone complex with MCM2, revealing how this dual histone and heat shock co-chaperone binds histone substrates. We show that DNAJC9 recruits HSP70-type enzymes via its J domain to fold histone H3-H4 substrates: upstream in the histone supply chain, during replication- and transcription-coupled nucleosome assembly, and to clean up spurious interactions. With its dual functionality, DNAJC9 integrates ATP-resourced protein folding into the his one supply pathway to resolve aberrant intermediates throughout the dynamic lives of histones.
HostingRepository	PRIDE
AnnounceDate	2022-02-14
AnnouncementXML	Submission_2022-02-14_02:19:43.909.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Ivo Hendriks
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive HF-X; Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2020-07-09 02:02:34	ID requested
1	2021-04-14 05:28:30	announced
2	2021-04-18 23:15:43	announced	2021-04-19: Updated project metadata.
⏵ 3	2022-02-14 02:19:44	announced	2022-02-14: Updated project metadata.
4	2024-10-22 05:21:09	announced	2024-10-22: Updated project metadata.

Hammond CM, Bao H, Hendriks IA, Carraro M, Garc, í, a-Nieto A, Liu Y, Rever, ó, n-G, ó, mez N, Spanos C, Chen L, Rappsilber J, Nielsen ML, Patel DJ, Huang H, Groth A, DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network. Mol Cell, 81(12):2533-2548.e9(2021) [pubmed]

ProteomeXchange project tag: EPIC-XS

submitter keyword: HSP70, histone chaperone,heat shock, HSP40,DNAJC9, chaperone

Michael Lund Nielsen
contact affiliation	Proteomics program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark
contact email	michael.lund.nielsen@cpr.ku.dk
lab head
Ivo Hendriks
contact affiliation	Proteomics program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen, Denmark
contact email	ivo.a.hendriks@gmail.com
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/2021/04/PXD020268

PRIDE project URI

• PRIDE
  1. PXD020268
     1. Label: PRIDE project
     2. Name: DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network