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The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules.


ABSTRACT: 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.

SUBMITTER: Collins RE 

PROVIDER: S-EPMC2586904 | biostudies-literature | 2008 Mar

REPOSITORIES: biostudies-literature

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The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules.

Collins Robert E RE   Northrop Jeffrey P JP   Horton John R JR   Lee David Y DY   Zhang Xing X   Stallcup Michael R MR   Cheng Xiaodong X  

Nature structural & molecular biology 20080210 3


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 lys  ...[more]

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