Evidence map›Paper›PMID 33741944›Full record

ArticleNature communications2021

Structural and dynamic mechanisms of CBF3-guided centromeric nucleosome formation.

Ruifang Guan, Tengfei Lian, Bing-Rui Zhou, Emily He, Carl Wu, Martin Singleton, Yawen Bai

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
5.5field-weighted citation impact, top 5% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
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  8. Beyond the mono-nucleosome.Biochemical Society transactions · 2025
    Review
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  10. Structure of yeast RAVE bound to a partial VProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. 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 4 institutions in 2 countries.

Ruifang Guan *Laboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Tengfei Lian *Laboratory of Membrane Proteins and Structural Biology, Biochemistry and Biophysics Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
Bing-Rui ZhouLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.ORCID 0000-0002-5375-7977
Emily HeJohn A. Paulson School of Engineering and Applied Sciences, Harvard University, Cambridge, MA, USA.
Carl WuDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA.ORCID 0000-0001-6933-5763
Martin SingletonStructural Biology of Chromosome Segregation Laboratory, The Francis Crick Institute, London, UK.ORCID 0000-0001-5716-7715
Yawen BaiLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA. baiyaw@mail.nih.gov.ORCID 0000-0003-3239-1109
National Institutes of Health · USHarvard University · USJohns Hopkins University · USThe Francis Crick Institute · GB

Funding

Nucleosome DynamicsZIABC010808 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BAI, YAWEN · 2009 to 2025
$26.5M
Cancer Research UK FC001155Medical Research Council FC001155Wellcome Trust FC001155
6 · The paper itself

Abstract

Accurate chromosome segregation relies on the specific centromeric nucleosome-kinetochore interface. In budding yeast, the centromere CBF3 complex guides the deposition of CENP-A, an H3 variant, to form the centromeric nucleosome in a DNA sequence-dependent manner. Here, we determine the structures of the centromeric nucleosome containing the native CEN3 DNA and the CBF3core bound to the canonical nucleosome containing an engineered CEN3 DNA. The centromeric nucleosome core structure contains 115 base pair DNA including a CCG motif. The CBF3core specifically recognizes the nucleosomal CCG motif through the Gal4 domain while allosterically altering the DNA conformation. Cryo-EM, modeling, and mutational studies reveal that the CBF3core forms dynamic interactions with core histones H2B and CENP-A in the CEN3 nucleosome. Our results provide insights into the structure of the budding yeast centromeric nucleosome and the mechanism of its assembly, which have implications for analogous processes of human centromeric nucleosome formation.

Indexed as

Amino Acid SequenceCentromereCentromere Protein ACryoelectron MicroscopyDNA-Binding ProteinsDNA, FungalHistonesHumansKinetochoresNucleic Acid ConformationNucleosomesProtein BindingProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidCBF2 protein, S cerevisiaeCentromere Protein ADNA-Binding ProteinsDNA, FungalHistonesNucleosomesSaccharomyces cerevisiae Proteins

Identifiers

PMID33741944
PMCPMC7979930
OpenAlexW3138222512

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LicenceCC BY
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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.