Evidence map›Paper›PMID 31848341›Full record

ArticleNature communications2019

Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone.

Carol Cho, Juwon Jang, Yujin Kang, Hiroki Watanabe, Takayuki Uchihashi, Seung Joong Kim, Koichi Kato, Ja Yil Lee, Ji-Joon Song

Open access · greenAbstract read
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

34 citing papers in PubMed, 34 citations in OpenAlex.

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  17. Visualization of the Cdc48 AAA+ ATPase protein unfolding pathway.bioRxiv : the preprint server for biology · 2023
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  19. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

Carol ChoDepartment of Biological Sciences and KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea. carol.cho@kaist.ac.kr.
Juwon JangDepartment of Biological Sciences and KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Yujin KangSchool of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan, Korea.
Hiroki WatanabeInstitute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, Japan.ORCID http://orcid.org/0000-0001-8547-1247
Takayuki UchihashiExploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of Natural Sciences, Okazaki, Japan.ORCID http://orcid.org/0000-0002-0263-5312
Seung Joong KimDepartment of Physics, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea.
Koichi KatoInstitute for Molecular Science (IMS), National Institutes of Natural Sciences, Okazaki, Japan.ORCID http://orcid.org/0000-0001-7187-9612
Ja Yil LeeSchool of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan, Korea. biojayil@unist.ac.kr.ORCID http://orcid.org/0000-0002-5726-9022
Ji-Joon SongDepartment of Biological Sciences and KI for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea. songj@kaist.ac.kr.ORCID http://orcid.org/0000-0001-7120-6311
Korea Advanced Institute of Science and Technology · KRNational Institutes of Natural Sciences · JPUlsan National Institute of Science and Technology · KRInstitute for Molecular Science · JP

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust
6 · The paper itself

Abstract

The fundamental unit of chromatin, the nucleosome, is an intricate structure that requires histone chaperones for assembly. ATAD2 AAA+ ATPases are a family of histone chaperones that regulate nucleosome density and chromatin dynamics. Here, we demonstrate that the fission yeast ATAD2 homolog, Abo1, deposits histone H3-H4 onto DNA in an ATP-hydrolysis-dependent manner by in vitro reconstitution and single-tethered DNA curtain assays. We present cryo-EM structures of an ATAD2 family ATPase to atomic resolution in three different nucleotide states, revealing unique structural features required for histone loading on DNA, and directly visualize the transitions of Abo1 from an asymmetric spiral (ATP-state) to a symmetric ring (ADP- and apo-states) using high-speed atomic force microscopy (HS-AFM). Furthermore, we find that the acidic pore of ATP-Abo1 binds a peptide substrate which is suggestive of a histone tail. Based on these results, we propose a model whereby Abo1 facilitates H3-H4 loading by utilizing ATP.

Indexed as

ATPases Associated with Diverse Cellular ActivitiesCryoelectron MicroscopyDNAHistone ChaperonesHistonesMicroscopy, Atomic ForceMolecular Dynamics SimulationNucleosomesProtein Conformation, alpha-HelicalProtein DomainsProtein Structure, QuaternaryRecombinant ProteinsSchizosaccharomyces pombe ProteinsSingle Molecule ImagingATPases Associated with Diverse Cellular ActivitiesDNAHistone ChaperonesHistonesNucleosomesRecombinant ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID31848341
PMCPMC6917787
OpenAlexW2996211626

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.