UNSPECIFIED (2000) Multiple histone acetyltransferases are associated with a chicken erythrocyte chromatin fraction enriched in active genes. JOURNAL OF BIOLOGICAL CHEMISTRY, 275 (40). pp. 31347-31352. ISSN 0021-9258

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Abstract

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 beta-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 tri-acetyl species; some acetylation of H2A can also be seen. Our results suggest that the chromatin-associated acetyltransferases have a role in gene regulation.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry
Journal or Publication Title:	JOURNAL OF BIOLOGICAL CHEMISTRY
Publisher:	AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
ISSN:	0021-9258
Date:	6 October 2000
Volume:	275
Number:	40
Number of Pages:	6
Page Range:	pp. 31347-31352
Publication Status:	Published
URI:	http://wrap.warwick.ac.uk/id/eprint/12887

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