Evidence map›Paper›PMID 17028330›Full record

ArticleGenetics2006

Phylogenetic analysis of fungal centromere H3 proteins.

Richard E Baker, Kelly Rogers

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

27 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Centromere drive: model systems and experimental progress.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2022
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
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  15. Article
  16. Article
  17. Review
  18. Centromeres of filamentous fungi.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2012
    Review
  19. Article
  20. Article
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

2 authors at 1 institution in 1 country.

Richard E BakerDepartment of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester, Massachusetts 01655, USA. richard.baker@umassmed.edu
Kelly Rogers
University of Massachusetts Chan Medical School · US

Funding

Assembling a Centric NucleosomeR01GM061120 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI BAKER, RICHARD E · 2001 to 2004
$1.1M
NIGMS NIH HHS GM61120NIGMS NIH HHS R01 GM061120
6 · The paper itself

Abstract

Centromere H3 proteins (CenH3's) are variants of histone H3 specialized for packaging centromere DNA. Unlike canonical H3, which is among the most conserved of eukaryotic proteins, CenH3's are rapidly evolving, raising questions about orthology and conservation of function across species. To gain insight on CenH3 evolution and function, a phylogenetic analysis was undertaken on CenH3 proteins drawn from a single, ancient lineage, the Fungi. Using maximum-likelihood methods, a credible phylogeny was derived for the conserved histone fold domain (HFD) of 25 fungal CenH3's. The collection consisted mostly of hemiascomycetous yeasts, but also included basidiomycetes, euascomycetes, and an archaeascomycete. The HFD phylogeny closely recapitulated known evolutionary relationships between the species, supporting CenH3 orthology. The fungal CenH3's lacked significant homology in their N termini except for those of the Saccharomyces/Kluyveromyces clade that all contained a region homologous to the essential N-terminal domain found in Saccharomyces cerevisiae Cse4. The ability of several heterologous CenH3's to function in S. cerevisiae was tested and found to correlate with evolutionary distance. Domain swapping between S. cerevisiae Cse4 and the noncomplementing Pichia angusta ortholog showed that species specificity could not be explained by the presence or absence of any recognized secondary structural element of the HFD.

Indexed as

PhylogenyAmino Acid SequenceCentromereDNA, FungalEvolution, MolecularFungal ProteinsGenes, FungalGenetic Complementation TestHistonesLikelihood FunctionsMolecular Sequence DataProtein FoldingProtein Structure, TertiarySaccharomyces cerevisiaeSequence Analysis, DNASequence Homology, Amino AcidDNA, FungalFungal ProteinsHistones

Identifiers

PMID17028330
PMCPMC1667059
OpenAlexW2139223623

What OpenQuestion holds

Textmetadata
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.