Characterization of the Histone H2A.Z-1 and H2A.Z-2 Isoforms in Vertebrates

Overview

Journal BMC Biol

Publisher Biomed Central

Specialty Biology

Date 2009 Dec 17

PMID 20003410

Citations 66

Authors

Deanna Dryhurst

Toyotaka Ishibashi

Kristie L Rose

Jose M Eirin-Lopez

Darin McDonald

Begonia Silva-Moreno

Nik Veldhoen

Caren C Helbing

Michael J Hendzel

Jeffrey Shabanowitz

Donald F Hunt

Juan Ausio

Affiliations

Soon will be listed here.

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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