Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Methods Mol Biol. 2012;809:465-72. doi: 10.1007/978-1-61779-376-9_30.

Affinity purification of MLL3/MLL4 histone H3K4 methyltransferase complex.

Author information

  • 1Nuclear Receptor Biology Section, NIDDK, NIH, Bethesda, MD, USA.

Abstract

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.

PMID:
22113294
[PubMed - indexed for MEDLINE]
PMCID:
PMC3467094
Free PMC Article

Images from this publication.See all images (1)Free text

Fig. 1
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Springer Icon for PubMed Central
    Loading ...
    Write to the Help Desk