AI Article Synopsis
- Histone methylation plays a crucial role in regulating chromatin function by influencing the chromatin structure and creating specific binding sites for proteins.
- Researchers studied the crystal structures of nucleosomes with methylated histones to understand how these modifications affect chromatin folding.
- Specifically, dimethylation of histone H3 at lysine 79 changes the nucleosome's immediate surface, while trimethylation of H4 at lysine 20 impacts the arrangement of nucleosome arrays at a higher level.
Article Abstract
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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Source |
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2648974 | PMC |
| http://dx.doi.org/10.1038/nsmb.1489 | DOI Listing |
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