The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure.
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.
Lu
Xu
X
Department of Biochemistry and Molecular Biology, Colorado State University, 1870 Campus Delivery, 1385 Center Avenue, Fort Collins, Colorado 80523-1870, USA.
Simon
Matthew D
MD
Chodaparambil
Jayanth V
JV
Hansen
Jeffrey C
JC
Shokat
Kevan M
KM
Luger
Karolin
K
D002843:Chromatin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D018360:Crystallography, X-Ray; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008239:Lysine / Q000235:genetics / Q000378:metabolism; D008745:Methylation; D008958:Models, Molecular; D009707:Nucleosomes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary
D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D008239:Lysine
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