Evidence map›Paper›PMID 19193230›Full record

ArticleBMC evolutionary biology2009

The evolutionary differentiation of two histone H2A.Z variants in chordates (H2A.Z-1 and H2A.Z-2) is mediated by a stepwise mutation process that affects three amino acid residues.

José M Eirín-López, Rodrigo González-Romero, Deanna Dryhurst, Toyotaka Ishibashi, Juan Ausió

Abstract read
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Article in BMC evolutionary biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

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0cells of the map it votes in
60citing papers in PubMed
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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

60 citing papers in PubMed.

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  15. Review
  16. Review
  17. Histone variants at a glance.Journal of cell science · 2021
    Review
  18. Article
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  20. Review
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

5 authors.

José M Eirín-LópezDepartamento de Biología Celular y Molecular, Universidade da Coruña, Coruña, Spain. jeirin@udc.es
Rodrigo González-Romero
Deanna Dryhurst
Toyotaka Ishibashi
Juan Ausió

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe histone H2A family encompasses the greatest number of core histone variants of which the replacement variant H2A.Z is currently one of the most heavily studied. No clear mechanism for the functional variability that H2A.Z imparts to chromatin has yet been proposed. While most of the past studies have referred to H2A.Z generically as a single protein, in vertebrates it is a mixture of two protein forms H2A.Z-1 (previously H2A.Z) and H2A.Z-2 (previously H2A.F/Z or H2A.V) that differ by three amino acids.

resultsWe have performed an extensive study on the long-term evolution of H2A.Z across metazoans with special emphasis on the possible selective mechanisms responsible for the differentiation between H2A.Z-1 and H2A.Z-2. Our results reveal a common origin of both forms early in chordate evolution. The evolutionary process responsible for the differentiation involves refined stepwise mutation change within the codons of the three differential residues. This eventually led to differences in the intensity of the selective constraints acting upon the different H2A.Z forms in vertebrates.

conclusionThe results presented in this work definitively reveal that the existence of H2A.Z-1 and H2A.Z-2 is not a whim of random genetic drift. Our analyses demonstrate that H2A.Z-2 is not only subject to a strong purifying selection but it is significantly more evolutionarily constrained than H2A.Z-1. Whether or not the evolutionary drift between H2A.Z-1 and H2A.Z-2 has resulted in a functional diversification of these proteins awaits further research. Nevertheless, the present work suggests that in the process of their differently constrained evolutionary pathways, these two forms may have acquired new or complementary functions.

Indexed as

Evolution, MolecularSelection, GeneticAmino Acid SequenceAnimalsChordataDatabases, GeneticGenetic DriftGenetic VariationHistonesLikelihood FunctionsModels, GeneticMolecular Sequence DataMutationPhylogenySequence AlignmentSpecies SpecificityHistones

Identifiers

PMID19193230
PMCPMC2644675

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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.