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Proteomics Data for "DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network"

UID: 10733

Description
Description from PRIDE: "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."
Subject of Study
Subject(s)
Access via PRIDE

RAW files of Proteome analysis available through FTP link or website download
Accession #: PXD020268

Access via ProteomeXchange

RAW files of Proteome analysis available through FTP link
Accession #: PXD020268

Access Restrictions
Free to All
Access Instructions
All public datasets available in PRIDE Archive in the repository can be accessed via the website by FTP link, Web Service (for programmatic access), and the PRIDE Inspector stand-alone tool.
Associated Publications
Equipment Used
Q Exactive
Q Exactive HF-X
Software Used
MaxQuant
Dataset Format(s)
RAW
Data Tool(s)
Mass Spectromety
Dataset Size
192.7 GB
Data Catalog Record Updated
2021-07-16