Evidence map›Paper›PMID 36744604›Full record

ArticleThe EMBO journal2023

The cryo-EM structure of the CENP-A nucleosome in complex with ggKNL2.

Honghui Jiang, Mariko Ariyoshi, Tetsuya Hori, Reito Watanabe, Fumiaki Makino, Keiichi Namba, Tatsuo Fukagawa

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
8.7field-weighted citation impact, top 3% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

  1. Dual Roads of CENP-A for Centromere Identification.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
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  8. Solution conformational differences between conventional and CENP-A nucleosomes are accentuated by reversible deformation under high pressure.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Article
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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

7 authors at 2 institutions in 1 country.

Honghui Jiang *Graduate School of Frontier Biosciences, Osaka University, Suita, Japan.ORCID 0000-0002-7487-9105
Mariko Ariyoshi *Graduate School of Frontier Biosciences, Osaka University, Suita, Japan.
Tetsuya HoriGraduate School of Frontier Biosciences, Osaka University, Suita, Japan.
Reito WatanabeGraduate School of Frontier Biosciences, Osaka University, Suita, Japan.
Fumiaki MakinoGraduate School of Frontier Biosciences, Osaka University, Suita, Japan.ORCID 0000-0001-9512-7087
Keiichi NambaGraduate School of Frontier Biosciences, Osaka University, Suita, Japan.ORCID 0000-0003-2911-5875
Tatsuo FukagawaGraduate School of Frontier Biosciences, Osaka University, Suita, Japan.ORCID 0000-0001-8564-6852
Ube Frontier University · JPJEOL (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Centromere protein A (CENP-A) nucleosomes containing the centromere-specific histone H3 variant CENP-A represent an epigenetic mark that specifies centromere position. The Mis18 complex is a licensing factor for new CENP-A deposition via the CENP-A chaperone, Holliday junction recognition protein (HJURP), on the centromere chromatin. Chicken KINETOCHORE NULL2 (KNL2) (ggKNL2), a Mis18 complex component, has a CENP-C-like motif, and our previous study suggested that ggKNL2 directly binds to the CENP-A nucleosome to recruit HJURP/CENP-A to the centromere. However, the molecular basis for CENP-A nucleosome recognition by ggKNL2 has remained unclear. Here, we present the cryo-EM structure of the chicken CENP-A nucleosome in complex with a ggKNL2 fragment containing the CENP-C-like motif. Chicken KNL2 distinguishes between CENP-A and histone H3 in the nucleosome using the CENP-C-like motif and its downstream region. Both the C-terminal tail and the RG-loop of CENP-A are simultaneously recognized as CENP-A characteristics. The CENP-A nucleosome-ggKNL2 interaction is thus essential for KNL2 functions. Furthermore, our structural, biochemical, and cell biology data indicate that ggKNL2 changes its binding partner at the centromere during chicken cell cycle progression.

Indexed as

HistonesNucleosomesAnimalsAutoantigensCell Cycle ProteinsCentromereCentromere Protein AChickensCryoelectron MicroscopyDNA-Binding ProteinsAutoantigensCell Cycle ProteinsCentromere Protein ADNA-Binding ProteinsHistonesNucleosomesCENP-ACENP-C-like motifCryo-EMKNL2

Identifiers

PMID36744604
PMCPMC10015371
OpenAlexW4319294898

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.