Evidence map›Paper›PMID 27225933›Full record

ArticleThe EMBO journal2016

Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly.

Carmen Aguilar-Gurrieri, Amédé Larabi, Vinesh Vinayachandran, Nisha A Patel, Kuangyu Yen, Rohit Reja, Ima-O Ebong, Guy Schoehn, Carol V Robinson, B Franklin Pugh and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
21.9field-weighted citation impact, top 1% 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

49 citing papers in PubMed, 77 citations in OpenAlex.

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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

11 authors at 4 institutions in 4 countries.

Carmen Aguilar-GurrieriEuropean Molecular Biology Laboratory, Grenoble, France Unit for Virus Host-Cell Interactions, Univ. Grenoble Alpes-EMBL-CNRS, Grenoble, France.
Amédé LarabiEuropean Molecular Biology Laboratory, Grenoble, France Unit for Virus Host-Cell Interactions, Univ. Grenoble Alpes-EMBL-CNRS, Grenoble, France.
Vinesh VinayachandranCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, USA.
Nisha A PatelDepartment of Chemistry, University of Oxford, Oxford, UK.
Kuangyu YenDepartment of Cell Biology, Southern Medical University, Guangzhou, China.
Rohit RejaCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, USA.
Ima-O EbongDepartment of Chemistry, University of Oxford, Oxford, UK.
Guy SchoehnUnit for Virus Host-Cell Interactions, Univ. Grenoble Alpes-EMBL-CNRS, Grenoble, France Université Grenoble-Alpes, Grenoble, France Centre National de la Recherche Scientifique (CNRS) IBS, Grenoble, France CEA, IBS, Grenoble, France.
Carol V RobinsonDepartment of Chemistry, University of Oxford, Oxford, UK.
B Franklin PughCenter for Eukaryotic Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA, USA.
Daniel PanneEuropean Molecular Biology Laboratory, Grenoble, France Unit for Virus Host-Cell Interactions, Univ. Grenoble Alpes-EMBL-CNRS, Grenoble, France panne@embl.fr.ORCID 0000-0001-9158-5507
Centre National de la Recherche Scientifique · FRPennsylvania State University · USUniversity of Oxford · GBSouthern Medical University · CN

Funding

High Resolution Mapping of Function Elements in the Yeast GenomeR01HG004160 · NHGRI · PENNSYLVANIA STATE UNIVERSITY, THE · PI PUGH, B FRANKLIN · 2007 to 2022
$5.3M
NHGRI NIH HHS R01 HG004160
6 · The paper itself

Abstract

Nap1 is a histone chaperone involved in the nuclear import of H2A-H2B and nucleosome assembly. Here, we report the crystal structure of Nap1 bound to H2A-H2B together with in vitro and in vivo functional studies that elucidate the principles underlying Nap1-mediated H2A-H2B chaperoning and nucleosome assembly. A Nap1 dimer provides an acidic binding surface and asymmetrically engages a single H2A-H2B heterodimer. Oligomerization of the Nap1-H2A-H2B complex results in burial of surfaces required for deposition of H2A-H2B into nucleosomes. Chromatin immunoprecipitation-exonuclease (ChIP-exo) analysis shows that Nap1 is required for H2A-H2B deposition across the genome. Mutants that interfere with Nap1 oligomerization exhibit severe nucleosome assembly defects showing that oligomerization is essential for the chaperone function. These findings establish the molecular basis for Nap1-mediated H2A-H2B deposition and nucleosome assembly.

Indexed as

Chromatin ImmunoprecipitationCrystallography, X-RayDNA Mutational AnalysisHistonesModels, MolecularNucleosome Assembly Protein 1NucleosomesProtein BindingProtein ConformationProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHistonesNAP1 protein, S cerevisiaeNucleosome Assembly Protein 1NucleosomesSaccharomyces cerevisiae ProteinschromatinH2A–H2Bhistone chaperoneNap1nucleosome assembly

Identifiers

PMID27225933
PMCPMC4931181
OpenAlexW2400443398

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.