Differentially methylated forms of histone H3 show unique association patterns with inactive human X chromosomes

Boggs, B. A., Cheung, P., Heard, E., Spector, D. L., Chinault, A. C., Allis, C. D. (January 2002) Differentially methylated forms of histone H3 show unique association patterns with inactive human X chromosomes. Nature Genetics, 30 (1). pp. 73-76. ISSN 1061-4036

URL: http://www.ncbi.nlm.nih.gov/pubmed/11740495
DOI: 10.1038/ng787


Studies of histone methylation have shown that H3 can be methylated at lysine 4 (Lys4) or lysine 9 (Lys9). Whereas H3-Lys4 methylation has been correlated with active gene expression, H3-Lys9 methylation has been linked to gene silencing and assembly of heterochromatin in mouse and Schizosaccharomyces pombe. The chromodomain of mouse HP1 (and Swi6 in S. pombe) binds H3 methylated at Lys9, and methylation at this site is thought to mark and promote heterochromatin assembly. We have used a well-studied model of mammalian epigenetic silencing, the human inactive X chromosome, to show that enrichment for H3 methylated at Lys9 is also a distinguishing mark of facultative heterochromatin. In contrast, H3 methylated at Lys4 is depleted in the inactive X chromosome, except in three 'hot spots' of enrichment along its length. Chromatin immunoprecipitation analyses further show that Lys9 methylation is associated with promoters of inactive genes, whereas Lys4 methylation is associated with active genes on the X chromosome. These data demonstrate that differential methylation at two distinct sites of the H3 amino terminus correlates with contrasting gene activities and may be part of a 'histone code' involved in establishing and maintaining facultative heterochromatin.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein methylation > histone methylation
CSHL Authors:
Communities: CSHL labs > Spector lab
Depositing User: Brian Soldo
Date: January 2002
Date Deposited: 04 Apr 2012 19:14
Last Modified: 29 Jan 2015 16:18
Related URLs:
URI: https://repository.cshl.edu/id/eprint/25645

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