Evaluation of Jumonji C lysine demethylase substrate preference to guide identification of in vitro substrates

Within the realm of lysine methylation, the discovery of lysine methyltransferase (KMTs) substrates has been burgeoning because of established systematic substrate screening protocols. Here, we describe a protocol enabling the systematic identification of JmjC KDM substrate preference and in vitro s...

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Detalles Bibliográficos
Autores principales: Hoekstra, Matthew, Chopra, Anand, Willmore, William G., Biggar, Kyle K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Protocol
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8976124/
https://www.ncbi.nlm.nih.gov/pubmed/35378885
http://dx.doi.org/10.1016/j.xpro.2022.101271
Descripción
Sumario:Within the realm of lysine methylation, the discovery of lysine methyltransferase (KMTs) substrates has been burgeoning because of established systematic substrate screening protocols. Here, we describe a protocol enabling the systematic identification of JmjC KDM substrate preference and in vitro substrates. Systematically designed peptide libraries containing methylated lysine residues are used to characterize enzyme-substrate preference and identify new candidate substrates in vitro. For complete details on the use and execution of this protocol, please refer to Hoekstra and Biggar (2021).

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