Article
An Ash2L/RbBP5 heterodimer stimulates the MLL1 methyltransferase activity through coordinated substrate interactions with the MLL1 SET domain.
PloS one - 23 Nov 2010
Cao Fang, Chen Yong, Cierpicki Tomasz, Liu Yifan, Basrur Venkatesha, Lei Ming, Dou Yali
Abstract excerpt
Histone H3 lysine 4 (K4) methylation is a prevalent mark associated with transcription activation and is mainly catalyzed by the MLL/SET1 family histone methyltransferases. A common feature of the mammalian MLL/SET1 complexes is the presence of three core components (RbBP5, Ash2L and WDR5) and a...
Topics
- Binding Sites
- DNA-Binding Proteins
- HeLa Cells
- Histone-Lysine N-Methyltransferase
- Histones
- Humans
- Immunoprecipitation
- Lysine
- Methylation
- Methyltransferases
- Models, Biological
- Mutation
- Myeloid-Lymphoid Leukemia Protein
- Nuclear Proteins