Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries

Noma, K., Allis, C. D., Grewal, S. I. S. (2001) Transitions in distinct histone H3 methylation patterns at the heterochromatin domain boundaries. Science, 293 (5532). pp. 1150-1155. ISSN 0036-8075

URL: http://www.ncbi.nlm.nih.gov/pubmed/11498594
DOI: 10.1126/science.1064150

Abstract

Eukaryotic genomes are organized into discrete structural and functional chromatin domains. Here, we show that distinct site-specific histone H3 methylation patterns define euchromatic and heterochromatic chromosomal domains within a 47-kilobase region of the mating-type locus in fission yeast. H3 methylated at lysine 9 (H3 Lys(9)), and its interacting Swi6 protein, are strictly localized to a 20-kilobase silent heterochromatic interval. In contrast, H3 methylated at lysine 4 (H3 LyS(4)) is specific to the surrounding euchromatic regions. Two inverted repeats flanking the silent interval serve as boundary elements to mark the borders between heterochromatin and euchromatin. Deletions of these boundary elements lead to spreading of H3 Lys(9) methylation and Swi6 into neighboring sequences. Furthermore, the H3 Lys(9) methylation and corresponding heterochromatin-associated complexes prevent H3 LyS(4) methylation in the silent domain.

Item Type: Paper
Uncontrolled Keywords: FISSION YEAST PROTEIN DIRECTIONALITY EXPRESSION CENTROMERE REGION LOCI
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosome
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosomes, structure and function > chromosome

bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > Chromatin dynamics > heterochromatin
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > histone
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein methylation > histone methylation
organism description > yeast
CSHL Authors:
Communities: CSHL labs > Grewal lab
Depositing User: Matt Covey
Date Deposited: 17 Jan 2014 20:37
Last Modified: 17 Jan 2014 20:37
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29278

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