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1: Nat Struct Mol Biol. 2008 Mar;15(3):245-50. Epub 2008 Feb 10.
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The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules.

Collins RE, Northrop JP, Horton JR, Lee DY, Zhang X, Stallcup MR, Cheng X.

Department of Biochemistry, Emory University School of Medicine, 1510 Clifton Road, Atlanta, Georgia 30322, USA.

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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PMID: 18264113 [PubMed - indexed for MEDLINE]