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In vitro enzyme assays for jmjC-domain-containing lysine histone demethylases (JmjC-KDMs)

Lookup NU author(s): Professor Akane Kawamura

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This is the authors' accepted manuscript of an article that has been published in its final definitive form by John Wiley & Sons, Inc., 2018.

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Abstract

© 2018 by John Wiley & Sons, Inc. Histone modifications, including lysine methylation marks on histone tails, modulate the accessibility of genes for transcription. Changes in histone tail methylation patterns can cause transcriptional activation or repression. The dynamic regulation of lysine methylation patterns is enabled by two distinct groups of enzymes: histone methyltransferases (KMTs) and demethylases (KDMs). The Jumonji C (JmjC) domain–containing lysine histone demethylases (JmjC-KDMs) alter the methylation levels of histone tails by removing tri-, di-, or mono-methylation marks. Because JmjC-KDMs activities are dysfunctional in cancer and other clinical conditions, they are targets for drug discovery. Efforts are underway to develop high-throughput assays capable of identifying selective, small-molecule inhibitors of KDMs. Detailed in this unit are protocols for mass spectrometry–based and formaldehyde dehydrogenase–coupled enzyme-based assays that can be used to identify inhibitors of JmjC-KDMs.

Publication metadata

Author(s): Tarhonskaya H, Tumber A, Kawamura A, Schofield CJ

Publication type: Article

Publication status: Published

Journal: Current Protocols in Pharmacology

Year: 2018

Volume: 80

Issue: 1

Pages: 3.15.1-3.15.12

Online publication date: 02/04/2018

Acceptance date: 02/04/2018

Date deposited: 14/10/2019

ISSN (print): 1934-8282

ISSN (electronic): 1934-8290

Publisher: John Wiley & Sons, Inc.

URL: https://doi.org/10.1002/cpph.34

DOI: 10.1002/cpph.34

PubMed id: 30040204

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