Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 15, Issue 10, Pages 1122-1124Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1489
Keywords
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Funding
- March of Dimes
- US National Institutes of Health (NIH) [GM067777, EB001987, GM45916]
- Howard Hughes Medical Institute
- NATIONAL INSTITUTE OF BIOMEDICAL IMAGING AND BIOENGINEERING [R01EB001987] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM067777, R01GM045916, R29GM045916] Funding Source: NIH RePORTER
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Histone methylation regulates chromatin function dependent on the site and degree of the modification. In addition to creating binding sites for proteins, methylated lysine residues are likely to influence chromatin structure directly. Here we present crystal structures of nucleosomes reconstituted with methylated histones and investigate the folding behavior of resulting arrays. We demonstrate that dimethylation of histone H3 at lysine residue 79 locally alters the nucleosomal surface, whereas trimethylation of H4 at lysine residue 20 affects higher-order structure.
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