Genomics

Dataset Information

0

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.

ORGANISM(S): Homo sapiens

PROVIDER: GSE154445 | GEO | 2021/04/14

REPOSITORIES: GEO

Dataset's files

Source:
Action DRS
Other
Items per page:
1 - 1 of 1

Similar Datasets

2021-04-14 | PXD020268 | Pride
2023-03-02 | PXD038263 | Pride
2023-03-02 | PXD034888 | Pride
2023-02-23 | PXD036809 | Pride
2024-07-29 | GSE269383 | GEO
2023-12-12 | PXD042390 | Pride
2023-12-10 | PXD042630 | Pride
2014-03-06 | PXD000686 | Pride
2021-12-02 | GSE183730 | GEO
2024-01-26 | PXD043392 | Pride