Human histone demethylase KDM6B can catalyse sequential oxidations

Jumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of Nε-methylated lysines on histones and play important roles in gene regulation. We report selectivity studies on KDM6B (JMJD3), a disease-relevant JmjC-KDM, using synthetic lysine analogues. The results unexpectedly reveal t...

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Published inChemical communications (Cambridge, England) Vol. 54; no. 57; pp. 7975 - 7978
Main Authors Hopkinson, Richard J, Langley, Gareth W, Belle, Roman, Walport, Louise J, Dunne, Kate, Münzel, Martin, Salah, Eidarus, Kawamura, Akane, Claridge, Timothy D W, Schofield, Christopher J
Format Journal Article
LanguageEnglish
Published England Royal Society of Chemistry 2018
Subjects
Alkylation
Amino Acid Sequence
Biocatalysis
Gene expression
Histones
Humans
Jumonji Domain-Containing Histone Demethylases - chemistry
Jumonji Domain-Containing Histone Demethylases - metabolism
Lysine
Lysine - metabolism
Oxidation-Reduction
Peptides - chemical synthesis
Peptides - metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Summary:Jumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of Nε-methylated lysines on histones and play important roles in gene regulation. We report selectivity studies on KDM6B (JMJD3), a disease-relevant JmjC-KDM, using synthetic lysine analogues. The results unexpectedly reveal that KDM6B accepts multiple Nε-alkylated lysine analogues, forming alcohol, aldehyde and carboxylic acid products.
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ISSN:1359-7345
1364-548X
DOI:10.1039/c8cc04057e