Human histone demethylase KDM6B can catalyse sequential oxidations

Jumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of N(ε)-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...

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Detalles Bibliográficos
Autores principales: 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.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2018
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6044289/
https://www.ncbi.nlm.nih.gov/pubmed/29961803
http://dx.doi.org/10.1039/c8cc04057e
Descripción
Sumario:Jumonji domain-containing demethylases (JmjC-KDMs) catalyse demethylation of N(ε)-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 N(ε)-alkylated lysine analogues, forming alcohol, aldehyde and carboxylic acid products.

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