Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates

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dc.contributor.authorDryhurst, Deanna
dc.contributor.authorIshibashi, Toyotaka
dc.contributor.authorRose, Kristie L.
dc.contributor.authorEirin-Lopez, Jose M.
dc.contributor.authorMcDonald, Darin
dc.contributor.authorSilva-Moreno, Begonia
dc.contributor.authorVeldhoen, Nik
dc.contributor.authorHelbing, Caren C.
dc.contributor.authorHendzel, Michael J.
dc.contributor.authorShabanowitz, Jeffrey
dc.contributor.authorHunt, Donald F.
dc.contributor.authorAusio, Juan
dc.date.accessioned2013-11-19T22:24:53Z
dc.date.available2013-11-19T22:24:53Z
dc.date.copyright2009en_US
dc.date.issued2009-12-14
dc.descriptionBioMed Centralen_US
dc.description.abstractBackground: Within chromatin, the histone variant H2A.Z plays a role in many diverse nuclear processes including transcription, preventing the spread of heterochromatin and epigenetic transcriptional memory. The molecular mechanisms of how H2A.Z mediates its effects are not entirely understood. However, it is now known that H2A.Z has two protein isoforms in vertebrates, H2A.Z-1 and H2A.Z-2, which are encoded by separate genes and differ by 3 amino acid residues. Results: We report that H2A.Z-1 and H2A.Z-2 are expressed across a wide range of human tissues, they are both acetylated at lysine residues within the N-terminal region and they exhibit similar, but nonidentical, distributions within chromatin. Our results suggest that H2A.Z-2 preferentially associates with H3 trimethylated at lysine 4 compared to H2A.Z-1. The phylogenetic analysis of the promoter regions of H2A.Z-1 and H2A.Z-2 indicate that they have evolved separately during vertebrate evolution. Conclusions: Our biochemical, gene expression, and phylogenetic data suggest that the H2A.Z-1 and H2A.Z-2 variants function similarly yet they may have acquired a degree of functional independence.en_US
dc.description.reviewstatusRevieweden_US
dc.description.scholarlevelFacultyen_US
dc.description.sponsorshipThis work was supported by a Canadian Institute of Health Research (CIHR) grant MOP-97878 (JA), a National Institute of Health Grant, GM 37537 (DFH), a CIHR grant (MH) and by a contract within the Ramon y Cajal Subprogramme (MICINN, Spain) (JME-L). MH is an Alberta Heritage Foundation for Medical Research Senior Scholar.en_US
dc.identifier.citationDryhurst et al. Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates. BMC Biology 2009 7:86en_US
dc.identifier.urihttp://www.biomedcentral.com/1741-7007/7/86
dc.identifier.urihttp://dx.doi.org/10.1186/1741-7007-7-86
dc.identifier.urihttp://hdl.handle.net/1828/5032
dc.language.isoenen_US
dc.publisherBioMed Centralen_US
dc.titleCharacterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebratesen_US
dc.typeArticleen_US

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