DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network Journal Article


Authors: Hammond, C. M.; Bao, H.; Hendriks, I. A.; Carraro, M.; García-Nieto, A.; Liu, Y.; Reverón-Gómez, N.; Spanos, C.; Chen, L.; Rappsilber, J.; Nielsen, M. L.; Patel, D. J.; Huang, H.; Groth, A.
Article Title: DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network
Abstract: 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 histone supply pathway to resolve aberrant intermediates throughout the dynamic lives of histones. © 2021 The Authors
Keywords: transcription; hsp70; histone chaperone; nucleosome assembly; chromatin replication; hsp40; dnajc9; heat shock co-chaperone; mcm2; tonsl
Journal Title: Molecular Cell
Volume: 81
Issue: 12
ISSN: 1097-2765
Publisher: Cell Press  
Date Published: 2021-06-17
Start Page: 2533
End Page: 2548.e9
Language: English
DOI: 10.1016/j.molcel.2021.03.041
PUBMED: 33857403
PROVIDER: scopus
PMCID: PMC8221569
DOI/URL:
Notes: Article -- Export Date: 1 July 2021 -- Source: Scopus
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  1. Dinshaw J Patel
    479 Patel