| RRC ID |
28670
|
| 著者 |
Tachibana M, Ueda J, Fukuda M, Takeda N, Ohta T, Iwanari H, Sakihama T, Kodama T, Hamakubo T, Shinkai Y.
|
| タイトル |
Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9.
|
| ジャーナル |
Genes Dev
|
| Abstract |
Histone H3 Lys 9 (H3-K9) methylation is a crucial epigenetic mark for transcriptional silencing. G9a is the major mammalian H3-K9 methyltransferase that targets euchromatic regions and is essential for murine embryogenesis. There is a single G9a-related methyltransferase in mammals, called GLP/Eu-HMTase1. Here we show that GLP is also important for H3-K9 methylation of mouse euchromatin. GLP-deficiency led to embryonic lethality, a severe reduction of H3-K9 mono- and dimethylation, the induction of Mage-a gene expression, and HP1 relocalization in embryonic stem cells, all of which were phenotypes of G9a-deficiency. Furthermore, we show that G9a and GLP formed a stoichiometric heteromeric complex in a wide variety of cell types. Biochemical analyses revealed that formation of the G9a/GLP complex was dependent on their enzymatic SET domains. Taken together, our new findings revealed that G9a and GLP cooperatively exert H3-K9 methyltransferase function in vivo, likely through the formation of higher-order heteromeric complexes.
|
| 巻・号 |
19(7)
|
| ページ |
815-26
|
| 公開日 |
2005-4-1
|
| DOI |
10.1101/gad.1284005
|
| PII |
gad.1284005
|
| PMID |
15774718
|
| PMC |
PMC1074319
|
| MeSH |
Animals
Euchromatin / enzymology*
Histone Methyltransferases
Histone-Lysine N-Methyltransferase / chemistry*
Histone-Lysine N-Methyltransferase / metabolism
Histones / metabolism*
Lysine / metabolism*
Methylation
Mice
Protein Methyltransferases
Protein Structure, Quaternary
Stem Cells / enzymology
|
| IF |
9.527
|
| 引用数 |
493
|
|
WOS 分野
|
GENETICS & HEREDITY
DEVELOPMENTAL BIOLOGY
CELL BIOLOGY
|
| リソース情報 |
| 遺伝子材料 |
14-1 (RDB05729) |
