The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote
- Dirk Schübeler1,7,8,
- David M. MacAlpine5,
- David Scalzo1,
- Christiane Wirbelauer7,
- Charles Kooperberg2,
- Fred van Leeuwen1,
- Daniel E. Gottschling1,
- Laura P. O'Neill6,
- Bryan M. Turner6,
- Jeffrey Delrow3,
- Stephen P. Bell5, and
- Mark Groudine1,4,8
- 1Division of Basic Sciences, 2Division of Public Health Sciences, and 3Genomics Resource, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA; 4Department of Radiation Oncology, University of Washington School of Medicine, Seattle, Washington 98195, USA; 5Department of Biology, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA; 6Chromatin and Gene Expression Group, Institute for Biomedical Research, University of Birmingham Medical School, Birmingham B152TT, UK; 7Friedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland
Abstract
The covalent modification of nucleosomal histones has emerged as a major determinant of chromatin structure and gene activity. To understand the interplay between various histone modifications, including acetylation and methylation, we performed a genome-wide chromatin structure analysis in a higher eukaryote. We found a binary pattern of histone modifications among euchromatic genes, with active genes being hyperacetylated for H3 and H4 and hypermethylated at Lys 4 and Lys 79 of H3, and inactive genes being hypomethylated and deacetylated at the same residues. Furthermore, the degree of modification correlates with the level of transcription, and modifications are largely restricted to transcribed regions, suggesting that their regulation is tightly linked to polymerase activity.
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Footnotes
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Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1198204.
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Supplemental material is available at http://www.genesdev.org.
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↵8 Corresponding authors. E-MAIL dirk{at}fmi.ch; markg{at}fhcrc.org; FAX 41-61-6973976.
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- Accepted April 14, 2004.
- Received February 24, 2004.
- Cold Spring Harbor Laboratory Press
