ArticleNucleic acids research2014
Scm3 deposits a (Cse4-H4)2 tetramer onto DNA through a Cse4-H4 dimer intermediate.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Direct observation of coordinated assembly of individual native centromeric nucleosomes.The EMBO journal · 2023Article
- Direct observation of coordinated assembly of individual native centromeric nucleosomes.bioRxiv : the preprint server for biology · 2023Article
- The Four Causes: The Functional Architecture of Centromeres and Kinetochores.Annual review of genetics · 2022Review
- The ATAD2/ANCCA homolog Yta7 cooperates with Scm3Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Conformational flexibility of histone variant CENP-AThe Journal of biological chemistry · 2018Article
- Histone chaperone networks shaping chromatin function.Nature reviews. Molecular cell biology · 2017Review
- Histone H4 Facilitates the Proteolysis of the Budding Yeast CENP-ACse4 Centromeric Histone Variant.Genetics · 2017Article
- In Vitro Chromatin Assembly: Strategies and Quality Control.Methods in enzymology · 2016Article
- The centromere: epigenetic control of chromosome segregation during mitosis.Cold Spring Harbor perspectives in biology · 2014Review
- Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The assembly of centromeric nucleosomes is mediated by histone variant-specific chaperones. In budding yeast, the centromere-specific histone H3 variant is Cse4, and the histone chaperone Scm3 functions as a Cse4-specific nucleosome assembly factor. Here, we show that Scm3 exhibits specificity for Cse4-H4, but also interacts with major-type H3-H4 and H2A-H2B. Previously published structures of the Scm3 histone complex demonstrate that Scm3 binds only one copy of Cse4-H4. Consistent with this, we show that Scm3 deposits Cse4-H4 through a dimer intermediate onto deoxyribonucleic acid (DNA) to form a (Cse4-H4)2-DNA complex (tetrasome). Scm3-bound Cse4-H4 does not form a tetramer in the absence of DNA. Moreover, we demonstrate that Cse4 and H3 are structurally compatible to be incorporated in the same nucleosome to form heterotypic particles. Our data shed light on the mechanism of Scm3-mediated nucleosome assembly at the centromere.
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Registered trials
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.