Evidence map›Paper›PMID 19782029›Full record

ArticleMolecular cell2009

Cse4 is part of an octameric nucleosome in budding yeast.

Raymond Camahort, Manjunatha Shivaraju, Mark Mattingly, Bing Li, Shima Nakanishi, Dongxiao Zhu, Ali Shilatifard, Jerry L Workman, Jennifer L Gerton

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
9.4field-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

111 citing papers in PubMed, 153 citations in OpenAlex.

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  11. Ccp1-Ndc80 switch at the N terminus of CENP-T regulates kinetochore assembly.Proceedings of the National Academy of Sciences of the United States of America · 2021
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  15. Article
  16. The ATAD2/ANCCA homolog Yta7 cooperates with Scm3Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Review
  19. Article
  20. Article

51 more citing papers are in PubMed but not listed here.

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.

Raymond CamahortStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Manjunatha Shivaraju
Mark Mattingly
Bing Li
Shima Nakanishi
Dongxiao Zhu
Ali Shilatifard
Jerry L Workman
Jennifer L Gerton
Stowers Institute for Medical Research · USUniversity of Kansas Medical Center · USThe Open University · GBUniversity of New Orleans · US

Funding

Physiological Role of MLL and ELL Proteins in LeukemiaR01CA089455 · NCI · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI SHILATIFARD, ALI · 2001 to 2015
$3.5M
Molecular Mechanisms of Chromosome Segregation in YeastR01GM080477 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI GERTON, JENNIFER L · 2008 to 2012
$1.5M
NCI NIH HHS R01 CA089455NIGMS NIH HHS R01 GM080477NIGMS NIH HHS R01GM080477
6 · The paper itself

Abstract

The budding yeast CenH3 histone variant Cse4 localizes to centromeric nucleosomes and is required for kinetochore assembly and chromosome segregation. The exact composition of centromeric Cse4-containing nucleosomes is a subject of debate. Using unbiased biochemical, cell-biological, and genetic approaches, we have tested the composition of Cse4-containing nucleosomes. Using micrococcal nuclease-treated chromatin, we find that Cse4 is associated with the histones H2A, H2B, and H4, but not H3 or the nonhistone protein Scm3. Overexpression of Cse4 rescues the lethality of a scm3 deletion, indicating that Scm3 is not essential for the formation of functional centromeric chromatin. We also find that octameric Cse4 nucleosomes can be reconstituted in vitro. Furthermore, Cse4-Cse4 dimerization occurs in vivo at the centromeric nucleosome, and this requires the predicted Cse4-Cse4 dimerization interface. Taken together, our experimental evidence supports the model that the Cse4 nucleosome is an octamer, containing two copies each of Cse4, H2A, H2B, and H4.

Indexed as

CentromereChromatin ImmunoprecipitationChromosomal Proteins, Non-HistoneDNA-Binding ProteinsGene Expression Regulation, FungalHistonesModels, MolecularMultiprotein ComplexesMutationNucleic Acid ConformationNucleosomesProtein ConformationProtein MultimerizationProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsChromosomal Proteins, Non-HistoneCSE4 protein, S cerevisiaeDNA-Binding ProteinsHistonesMultiprotein ComplexesNucleosomesProtein SubunitsSaccharomyces cerevisiae Proteins

Identifiers

PMID19782029
PMCPMC2757638
OpenAlexW2019180618

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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.