1. Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates
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Deanna Dryhurst, Toyotaka Ishibashi, Jeffrey Shabanowitz, Caren C. Helbing, Michael J. Hendzel, Darin McDonald, Nik Veldhoen, Kristie L. Rose, José M. Eirín-López, Donald F. Hunt, Juan Ausió, and Begonia Silva-Moreno
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Gene isoform ,animal structures ,Euchromatin ,Physiology ,Heterochromatin ,Plant Science ,Biology ,Methylation ,General Biochemistry, Genetics and Molecular Biology ,Avian Proteins ,Histones ,03 medical and health sciences ,Mice ,Species Specificity ,Structural Biology ,Gene expression ,Research article ,Animals ,Humans ,Protein Isoforms ,Epigenetics ,RNA, Messenger ,Promoter Regions, Genetic ,Gene ,lcsh:QH301-705.5 ,Ecology, Evolution, Behavior and Systematics ,Cells, Cultured ,030304 developmental biology ,Genetics ,0303 health sciences ,Agricultural and Biological Sciences(all) ,Biochemistry, Genetics and Molecular Biology(all) ,030302 biochemistry & molecular biology ,Acetylation ,Cell Biology ,Biological Evolution ,Macaca mulatta ,Chromatin ,Histone ,lcsh:Biology (General) ,embryonic structures ,biology.protein ,General Agricultural and Biological Sciences ,Chickens ,Developmental Biology ,Biotechnology ,HeLa Cells - Abstract
Background 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.
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