Evidence map›Paper›PMID 33857403›Full record

ArticleMolecular cell2021

DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network.

Colin M Hammond, Hongyu Bao, Ivo A Hendriks, Massimo Carraro, Alberto García-Nieto, Yanhong Liu, Nazaret Reverón-Gómez, Christos Spanos, Liu Chen, Juri Rappsilber and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
6.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 85 citations in OpenAlex.

  1. Review
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  4. Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026
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  16. DNA polymerase delta governs parental histone transfer to DNA replication lagging strand.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 4 institutions in 5 countries.

Colin M HammondNovo Nordisk Foundation Center for Protein Research (CPR), University of Copenhagen, Copenhagen, Denmark; Biotech Research and Innovation Centre (BRIC), University of Copenhagen, Copenhagen, Denmark.
Hongyu BaoKey Laboratory of Molecular Design for Plant Cell Factory of Guangdong Higher Education Institutes, Department of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen 518055, China.
Ivo A HendriksNovo Nordisk Foundation Center for Protein Research (CPR), University of Copenhagen, Copenhagen, Denmark.
Massimo CarraroNovo Nordisk Foundation Center for Protein Research (CPR), University of Copenhagen, Copenhagen, Denmark; Biotech Research and Innovation Centre (BRIC), University of Copenhagen, Copenhagen, Denmark.
Alberto García-NietoBiotech Research and Innovation Centre (BRIC), University of Copenhagen, Copenhagen, Denmark.
Yanhong LiuKey Laboratory of Molecular Design for Plant Cell Factory of Guangdong Higher Education Institutes, Department of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen 518055, China.
Nazaret Reverón-GómezNovo Nordisk Foundation Center for Protein Research (CPR), University of Copenhagen, Copenhagen, Denmark; Biotech Research and Innovation Centre (BRIC), University of Copenhagen, Copenhagen, Denmark.
Christos SpanosWellcome Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.
Liu ChenKey Laboratory of Molecular Design for Plant Cell Factory of Guangdong Higher Education Institutes, Department of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen 518055, China.
Juri RappsilberWellcome Centre for Cell Biology, University of Edinburgh, Edinburgh, UK; Bioanalytics, Institute of Biotechnology, Technische Universität Berlin, Berlin, Germany.
Michael L NielsenNovo Nordisk Foundation Center for Protein Research (CPR), University of Copenhagen, Copenhagen, Denmark.
Dinshaw J PatelStructural Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA. Electronic address: pateld@mskcc.org.
Hongda HuangKey Laboratory of Molecular Design for Plant Cell Factory of Guangdong Higher Education Institutes, Department of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen 518055, China. Electronic address: huanghd@sustech.edu.cn.
Anja GrothNovo Nordisk Foundation Center for Protein Research (CPR), University of Copenhagen, Copenhagen, Denmark; Biotech Research and Innovation Centre (BRIC), University of Copenhagen, Copenhagen, Denmark. Electronic address: anja.groth@cpr.ku.dk.
University of Copenhagen · DKSouthern University of Science and Technology · CNWellcome Centre for Cell Biology · GBMemorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
NCI NIH HHS P30 CA008748Wellcome TrustWellcome Trust 103139Wellcome Trust 203149
6 · The paper itself

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.

Indexed as

Cell Line, TumorChromatinChromatin Assembly and DisassemblyDNA ReplicationHeLa CellsHistone ChaperonesHistonesHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansMinichromosome Maintenance Complex Component 2Models, MolecularMolecular ChaperonesNucleosomesProtein BindingProteomicsChromatinDNAJC9 protein, humanHistone ChaperonesHistonesHSP40 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsMCM2 protein, humanMinichromosome Maintenance Complex Component 2Molecular ChaperonesNucleosomeschromatin replicationDNAJC9heat shock co-chaperonehistone chaperoneHSP40HSP70MCM2nucleosome assemblyTONSLtranscription

Identifiers

PMID33857403
PMCPMC8221569
OpenAlexW3154637679

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.