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Transcriptional Regulation pp 465–472Cite as

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

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Part of the book series: Methods in Molecular Biology ((MIMB,volume 809))

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.

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Authors and Affiliations

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

    Young-Wook Cho, SunHwa Hong & Kai Ge

Authors
  1. Young-Wook Cho
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  2. SunHwa Hong
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  3. Kai Ge
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Corresponding author

Correspondence to Kai Ge .

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Editors and Affiliations

  1. , Department of Biological Sciences, St. John's University, Utopia Parkway 8000, Queens, 11439, New York, USA

    Ales Vancura

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Cho, YW., Hong, S., Ge, K. (2012). Affi nity Purifi cation of MLL3/MLL4 Histone H3K4 Methyltransferase Complex. In: Vancura, A. (eds) Transcriptional Regulation. Methods in Molecular Biology, vol 809. Springer, New York, NY. https://doi.org/10.1007/978-1-61779-376-9_30

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  • DOI: https://doi.org/10.1007/978-1-61779-376-9_30

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  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-61779-375-2

  • Online ISBN: 978-1-61779-376-9

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