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.
journal_name
BMC Bioljournal_title
BMC biologyauthors
Dryhurst D,Ishibashi T,Rose KL,Eirín-López JM,McDonald D,Silva-Moreno B,Veldhoen N,Helbing CC,Hendzel MJ,Shabanowitz J,Hunt DF,Ausió Jdoi
10.1186/1741-7007-7-86subject
Has Abstractpub_date
2009-12-14 00:00:00pages
86issn
1741-7007pii
1741-7007-7-86journal_volume
7pub_type
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