Isolation and characterization of histone H3 lysine 4 demethylase-containing complexes

Min Gyu Lee, Christopher Wynder, Jessica Norman, Ramin Shiekhattar

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Histone methylation is involved in the regulation of many cellular processes. In the past 2 years, several histone demethylases including BHC110/LSD1 have been characterized. BHC110, the first known histone lysine demethylase, removes methyl groups from methylated histone H3 lysine 4 and has been found in many multi-protein complexes. Using one-step affinity purification, we have isolated enzymatically active BHC110-containing complexes. Here, we detail the methods used for the isolation and characterization of these histone demethylase complexes from a human stable cell line.

Original languageEnglish (US)
Pages (from-to)327-330
Number of pages4
JournalMethods
Volume40
Issue number4
DOIs
StatePublished - Dec 2006
Externally publishedYes

Fingerprint

Histone Demethylases
Histones
Lysine
Methylation
Purification
Cells
Cell Line
Proteins

Keywords

  • BHC110/LSD1
  • Histone demethylase
  • Histone methylation
  • Protein complex

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Isolation and characterization of histone H3 lysine 4 demethylase-containing complexes. / Lee, Min Gyu; Wynder, Christopher; Norman, Jessica; Shiekhattar, Ramin.

In: Methods, Vol. 40, No. 4, 12.2006, p. 327-330.

Research output: Contribution to journalArticle

Lee, Min Gyu ; Wynder, Christopher ; Norman, Jessica ; Shiekhattar, Ramin. / Isolation and characterization of histone H3 lysine 4 demethylase-containing complexes. In: Methods. 2006 ; Vol. 40, No. 4. pp. 327-330.
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