Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases

Louise J. Walport; Richard J. Hopkinson; Rasheduzzaman Chowdhury; Rachel Schiller; Wei Ge; Akane Kawamura; Christopher J. Schofield

doi:10.1038/ncomms11974

Nature Communications (Jun 2016)

Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases

Louise J. Walport,
Richard J. Hopkinson,
Rasheduzzaman Chowdhury,
Rachel Schiller,
Wei Ge,
Akane Kawamura,
Christopher J. Schofield

Affiliations

Louise J. Walport: Department of Chemistry, Chemistry Research Laboratory, University of Oxford
Richard J. Hopkinson: Department of Chemistry, Chemistry Research Laboratory, University of Oxford
Rasheduzzaman Chowdhury: Department of Chemistry, Chemistry Research Laboratory, University of Oxford
Rachel Schiller: Department of Chemistry, Chemistry Research Laboratory, University of Oxford
Wei Ge: Department of Chemistry, Chemistry Research Laboratory, University of Oxford
Akane Kawamura: Department of Chemistry, Chemistry Research Laboratory, University of Oxford
Christopher J. Schofield: Department of Chemistry, Chemistry Research Laboratory, University of Oxford

DOI: https://doi.org/10.1038/ncomms11974
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 12

Abstract

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While reversal of lysine methylation on histone tails is a well-established mechanism to tune gene expression, the existence of a similar arginine demethylation process is controversial. Here, the authors show that some jumonji enzymes possess both lysine and arginine demethylase activity in vitro.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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