Cited by 70Genomics and Chromatin DynamicsEpigenetics and DNA MethylationHemoglobinopathies and Related Disorders

Identification of a conserved erythroid specific domain of histone acetylation across the α-globin gene cluster

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Anguita, Eduardo, Johnson, Colin A., Wood, William G., Turner, Bryan M., Higgs, Douglas R.·2001·Proceedings of the National Academy of Sciences

Abstract

We have analyzed the pattern of core histone acetylation across 250 kb of the telomeric region of the short arm of human chromosome 16. This gene-dense region, which includes the α-globin genes and their regulatory elements embedded within widely expressed genes, shows marked differences in histone acetylation between erythroid and non-erythroid cells. In non-erythroid cells, there was a uniform 2- to 3-fold enrichment of acetylated histones, compared with heterochromatin, across the entire region. In erythroid cells, an ≈100-kb segment of chromatin encompassing the α genes and their remote major regulatory element was highly enriched in histone H4 acetylated at Lys-5. Other lysines in the N-terminal tail of histone H4 showed intermediate and variable levels of enrichment. Similar broad segments of erythroid-specific histone acetylation were found in the corresponding syntenic regions containing the mouse and chicken α-globin gene clusters. The borders of these regions of acetylation are located in similar positions in all three species, and a sharply defined 3′ boundary coincides with the previously identified breakpoint in conserved synteny between these species. We have therefore demonstrated that an erythroid-specific domain of acetylation has been conserved across several species, encompassing not only the α-globin genes but also a neighboring widely expressed gene. These results contrast with those at other clusters and demonstrate that not all genes are organized into discrete regulatory domains.

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Crossref · 10.1073/pnas.201413098

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  • Activation of α-globin expression in erythroid cells is associated with the appearance of a broad domain of histone acetylation and H3K4me1 spanning ~80kb including the α-globin genes and their regulatory elements.

    “activation of α-globin expression in erythroid cells is associated with the appearance of a broad domain of histone acetylation and modification by H3K4me1 spanning ~80kb including the α-globin genes and their regulatory elements (Fig. 1B)13,14.”

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Authors
Anguita, E., Johnson, C. A., Wood, W. G., Turner, B. M., & Higgs, D. R.
Affiliations
John Radcliffe Hospital (GB)
Venue
Proceedings of the National Academy of Sciences
Published
2001-10-02
Volume
98
Issue
21
Pages
12114-12119
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2067137429
Cited by
70
References
51
Citations by year
2021: 1 · 2019: 1 · 2017: 2 · 2016: 3 · 2015: 1 · 2014: 2 · 2013: 1 · 2012: 3
FWCI
2.56
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • University of Birmingham Research Portal (University of Birmingham) (submittedVersion)
Funders
Wellcome Trust
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
  • Health Sciences › Medicine › Genetics › Hemoglobinopathies and Related Disorders
Keywords
histone acetylation, alpha-globin gene cluster, heterochromatin, synteny conservation, chromatin organization
MeSH terms
Acetylation, Animals, Binding Sites, Cell Line, Transformed, Chickens, Chromosomes, Human, Pair 16, Erythrocytes, Multigene Family, Globins, Histones, Humans, Tumor Cells, Cultured, Conserved Sequence, K562 Cells, Synteny, Mice

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