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."
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Access via PRIDE
RAW files of Proteome analysis available through FTP link or website download
Accession #: PXD020268Access via ProteomeXchangeRAW files of Proteome analysis available through FTP link
Accession #: PXD020268 - Access Restrictions
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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
- Software Used
- Dataset Format(s)
- RAW
- Data Tool(s)
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Mass Spectromety
- Dataset Size
- 192.7 GB
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