期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 15, 期 3, 页码 245-250出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1384
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资金
- NIDDK NIH HHS [R37 DK055274-10, R37 DK055274, R01 DK055274, DK55274] Funding Source: Medline
- NIGMS NIH HHS [R01 GM068680, GM068680] Funding Source: Medline
Histone modifications have important roles in transcriptional control, mitosis and heterochromatin formation. G9a and G9a-like protein (GLP) are euchromatin-associated methyltransferases that repress transcription by mono- and dimethylating histone H3 at Lys9 (H3K9). Here we demonstrate that the ankyrin repeat domains of G9a and GLP bind with strong preference to N-terminal H3 peptides containing mono- or dimethyl K9. X-ray crystallography revealed the basis for recognition of the methylated lysine by a partial hydrophobic cage with three tryptophans and one acidic residue. Substitution of key residues in the cage eliminated the H3 tail interaction. Hence, G9a and GLP contain a new type of methyllysine binding module (the ankyrin repeat domains) and are the first examples of protein (histone) methyltransferases harboring in a single polypeptide the activities that generate and read the same epigenetic mark.
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