3SWC

GLP (G9a-like protein) SET domain in complex with Dnmt3aK44me2 peptide

Summary for 3SWC

• Entry DOI: 10.2210/pdb3swc/pdb
• Related: 3SVM 3SW9
• Descriptor: Histone-lysine N-methyltransferase EHMT1, DNA (cytosine-5)-methyltransferase 3A, ZINC ION, ... (5 entities in total)
• Functional Keywords: epigenetics, non-histone lysine methylation, set domain, protein lysine methyltransferase, transferase
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q9H9B1 O88508
• Total number of polymer chains: 4
• Total formula weight: 69525.55

Authors

Chang, Y.,Horton, J.R.,Zhang, X.,Cheng, X. (deposition date: 2011-07-13, release date: 2011-11-30, Last modification date: 2023-09-13)

Primary citation

Chang, Y.,Sun, L.,Kokura, K.,Horton, J.R.,Fukuda, M.,Espejo, A.,Izumi, V.,Koomen, J.M.,Bedford, M.T.,Zhang, X.,Shinkai, Y.,Fang, J.,Cheng, X.
MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a.
Nat Commun, 2:533-533, 2011

PubMed Abstract: DNA CpG methylation and histone H3 lysine 9 (H3K9) methylation are two major repressive epigenetic modifications, and these methylations are positively correlated with one another in chromatin. Here we show that G9a or G9a-like protein (GLP) dimethylate the amino-terminal lysine 44 (K44) of mouse Dnmt3a (equivalent to K47 of human DNMT3A) in vitro and in cells overexpressing G9a or GLP. The chromodomain of MPP8 recognizes the dimethylated Dnmt3aK44me2. MPP8 also interacts with self-methylated GLP in a methylation-dependent manner. The MPP8 chromodomain forms a dimer in solution and in crystals, suggesting that a dimeric MPP8 molecule could bridge the methylated Dnmt3a and GLP, resulting in a silencing complex of Dnmt3a-MPP8-GLP/G9a on chromatin templates. Together, these findings provide a molecular explanation, at least in part, for the co-occurrence of DNA methylation and H3K9 methylation in chromatin.

PubMed: 22086334
DOI: 10.1038/ncomms1549

Experimental method

X-RAY DIFFRACTION (2.332 Å)