Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates
Date
2009-12-14
Authors
Dryhurst, Deanna
Ishibashi, Toyotaka
Rose, Kristie L.
Eirin-Lopez, Jose M.
McDonald, Darin
Silva-Moreno, Begonia
Veldhoen, Nik
Helbing, Caren C.
Hendzel, Michael J.
Shabanowitz, Jeffrey
Journal Title
Journal ISSN
Volume Title
Publisher
BioMed Central
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.
Description
BioMed Central
Keywords
Citation
Dryhurst et al. Characterization of the histone H2A.Z-1 and H2A.Z-2 isoforms in vertebrates. BMC Biology 2009 7:86