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DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network.
<div class='caption-title'>Identification of DNAJC9 as a dual histone chaperone and heat shock co-chaperone</div>
<div class='caption-title'>Structure of DNAJC9 and MCM2 bound simultaneously to an H3.3-H4 dimer</div>
Hammond CM, Bao H, Hendriks IA, Carraro M, García-Nieto A, Liu Y, Reverón-Gómez N, Spanos C, Chen L, Rappsilber J, Nielsen ML, Patel DJ, Huang H, Groth A
OpenAccess logo Mol Cell 81 2533-2548.e9 (2021)
Cited: 18 times
EuropePMC logo PMID: 33857403

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.

Articles - 7cj0 mentioned but not cited (1)

  1. DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network. Hammond CM, Bao H, Hendriks IA, Carraro M, García-Nieto A, Liu Y, Reverón-Gómez N, Spanos C, Chen L, Rappsilber J, Nielsen ML, Patel DJ, Huang H, Groth A. Mol Cell 81 2533-2548.e9 (2021)


Reviews citing this publication (3)

  1. Regulation of p53 and Cancer Signaling by Heat Shock Protein 40/J-Domain Protein Family Members. Kaida A, Iwakuma T. Int J Mol Sci 22 13527 (2021)
  2. The Astonishing Large Family of HSP40/DnaJ Proteins Existing in Leishmania. Solana JC, Bernardo L, Moreno J, Aguado B, Requena JM. Genes (Basel) 13 742 (2022)
  3. Interaction of client-the scaffold on which FeS clusters are build-with J-domain protein Hsc20 and its evolving Hsp70 partners. Marszalek J, Craig EA. Front Mol Biosci 9 1034453 (2022)

Articles citing this publication (14)



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