Multiple Histone Acetyltransferases Are Associated with a Chicken Erythrocyte Chromatin Fraction Enriched in Active Genes

We have examined salt-soluble chromatin released by micrococcal nuclease from a 15-day-old chicken embryo erythrocyte nuclei for histone acetyltransferase (HAT) activities. This chromatin is enriched in transcriptionally active sequences from within the active β-globin locus and contains elevated le...

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Bibliographic Details
Published in:The Journal of biological chemistry 2000-10, Vol.275 (40), p.31347-31352
Main Authors: Hebbes, Tim R., Allen, Stuart C.H.
Format: Article
Language:English
Subjects:
Acetylation
Acetyltransferases - chemistry
Acetyltransferases - metabolism
Animals
Blotting, Southern
Cell Nucleus - chemistry
Cell Nucleus - metabolism
Centrifugation, Density Gradient
Chick Embryo
Chromatin - chemistry
Chromatin - metabolism
Electrophoresis, Polyacrylamide Gel
Erythrocytes - chemistry
Histone Acetyltransferases
Histones - metabolism
Micrococcal Nuclease - metabolism
Nucleic Acid Hybridization
Protein Binding
Saccharomyces cerevisiae Proteins
Salts - metabolism
Transcription, Genetic
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Summary:We have examined salt-soluble chromatin released by micrococcal nuclease from a 15-day-old chicken embryo erythrocyte nuclei for histone acetyltransferase (HAT) activities. This chromatin is enriched in transcriptionally active sequences from within the active β-globin locus and contains elevated levels of acetylated core histones. HAT activities present in this fraction target histones H4, H3, and H2A when the chromatin itself is used as the substrate. In gel HAT activity assay demonstrates that the salt-soluble chromatin fraction contains four acetyltransferase molecules distinguished by their different molecular masses (47, 33, 32, and 28 kDa). Further separation of the chromatin by centrifugation through sucrose gradients shows that the acetyltransferases segregate into chromatin-bound and chromatin-free populations. The 32- and 28-kDa HATs are associated with chromatin, whereas the 47- and 33-kDa HAT molecules are not. The chromatin-bound HAT activities predominantly target H4 to give the diacetyl and triacetyl species; some acetylation of H2A can also be seen. Our results suggest that the chromatin-associated acetyltransferases have a role in gene regulation.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M004830200