Transcriptional Regulation

Volume 809 of the series Methods in Molecular Biology pp 465-472


Affi nity Purifi cation of MLL3/MLL4 Histone H3K4 Methyltransferase Complex

  • Young-Wook ChoAffiliated withNuclear Receptor Biology Section, NIDDK, NIH
  • , SunHwa HongAffiliated withNuclear Receptor Biology Section, NIDDK, NIH
  • , Kai GeAffiliated withNuclear Receptor Biology Section, NIDDK, NIH Email author 

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Methylation on histone H3 lysine 4 (H3K4) correlates with actively transcribed genes. In mammalian cells, there exist multiple Set1-like histone H3K4 methyltransferase complexes, which have overlapping but distinct subunit compositions. Developing methods to isolate each of these histone H3K4 methyltransferase complexes would help understand the molecular mechanisms by which histone H3K4 methylation regulates mammalian gene expression. In this chapter, we provide a one-step affinity purification protocol on isolation of the MLL3/MLL4 histone H3K4 methyltransferase complex using FLAG-tagged PA1, a unique subunit of the MLL3/MLL4 complex.

Key words

Histone H3K4 methyltransferase complex MLL3 MLL4 PA1