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

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

doi:10.1016/j.ymeth.2006.07.030

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

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

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

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 language	English (US)
Pages (from-to)	327-330
Number of pages	4
Journal	Methods
Volume	40
Issue number	4
DOIs	https://doi.org/10.1016/j.ymeth.2006.07.030
State	Published - Dec 2006
Externally published	Yes

Keywords

BHC110/LSD1
Histone demethylase
Histone methylation
Protein complex

ASJC Scopus subject areas

Molecular Biology
General Biochemistry, Genetics and Molecular Biology

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10.1016/j.ymeth.2006.07.030

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title = "Isolation and characterization of histone H3 lysine 4 demethylase-containing complexes",

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.",

keywords = "BHC110/LSD1, Histone demethylase, Histone methylation, Protein complex",

author = "Lee, {Min Gyu} and Christopher Wynder and Jessica Norman and Ramin Shiekhattar",

note = "Funding Information: R.S. was supported by a grant from NIH (GM61204).",

year = "2006",

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doi = "10.1016/j.ymeth.2006.07.030",

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pages = "327--330",

journal = "Methods",

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T1 - Isolation and characterization of histone H3 lysine 4 demethylase-containing complexes

AU - Lee, Min Gyu

AU - Wynder, Christopher

AU - Norman, Jessica

AU - Shiekhattar, Ramin

N1 - Funding Information: R.S. was supported by a grant from NIH (GM61204).

PY - 2006/12

Y1 - 2006/12

N2 - 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.

AB - 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.

KW - BHC110/LSD1

KW - Histone demethylase

KW - Histone methylation

KW - Protein complex

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DO - 10.1016/j.ymeth.2006.07.030

M3 - Article

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AN - SCOPUS:33750728922

SN - 1046-2023

VL - 40

SP - 327

EP - 330

JO - Methods

JF - Methods

IS - 4

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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