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

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dc.contributor.authorEirin-Lopez, Jose M.
dc.contributor.authorGonzalez-Romero, Rodrigo
dc.contributor.authorDryhurst, Deanna
dc.contributor.authorIshibashi, Toyotaka
dc.contributor.authorAusio, Juan
dc.date.accessioned2013-11-19T22:30:25Z
dc.date.available2013-11-19T22:30:25Z
dc.date.copyright2009en_US
dc.date.issued2009-02-04
dc.descriptionBioMed Centralen_US
dc.description.abstractBackground: The 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. Results: We 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. Conclusion: The 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.en_US
dc.description.reviewstatusRevieweden_US
dc.description.scholarlevelFacultyen_US
dc.description.sponsorshipThis work was funded in part by a Canadian Institutes of Health Research (CIHR) Grant MOP-57718 to J.A. and by a Marie Curie Outgoing International Fellowship (MOIF-CT-2005-021900) within the 6th Framework Programme (European Union) and by a contract within the Isidro Parga Pondal Program (Xunta de Galicia) to J.M.E.-L. R.G.-R. Holds a fellowship from the Diputacion de A Coruña (Spain) and a Predoctoral fellowship from the Universidade da Coruña and T.I. holds a Michael Smith Foundation for Health Research (MSFHR) Postdoctoral Fellowship.en_US
dc.identifier.citationEirin-Lopez et al. 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 aminio acid residues. BMC Evolutionary Biology 2009 9:31en_US
dc.identifier.urihttp://www.biomedcentral.com/1471-2148/9/31
dc.identifier.urihttp://dx.doi.org/10.1186/1471-2148-9-31
dc.identifier.urihttp://hdl.handle.net/1828/5033
dc.language.isoenen_US
dc.publisherBioMed Centralen_US
dc.subject.departmentDepartment of Biochemistry and Microbiology
dc.titleThe 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 residuesen_US
dc.typeArticleen_US

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