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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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
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author Hoekstra, Matthew
Chopra, Anand
Willmore, William G.
Biggar, Kyle K.
author_facet Hoekstra, Matthew
Chopra, Anand
Willmore, William G.
Biggar, Kyle K.
author_sort Hoekstra, Matthew
collection PubMed
description 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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spelling pubmed-89761242022-04-03 Evaluation of Jumonji C lysine demethylase substrate preference to guide identification of in vitro substrates Hoekstra, Matthew Chopra, Anand Willmore, William G. Biggar, Kyle K. STAR Protoc Protocol 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). Elsevier 2022-03-30 /pmc/articles/PMC8976124/ /pubmed/35378885 http://dx.doi.org/10.1016/j.xpro.2022.101271 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Protocol
Hoekstra, Matthew
Chopra, Anand
Willmore, William G.
Biggar, Kyle K.
Evaluation of Jumonji C lysine demethylase substrate preference to guide identification of in vitro substrates
title Evaluation of Jumonji C lysine demethylase substrate preference to guide identification of in vitro substrates
title_full Evaluation of Jumonji C lysine demethylase substrate preference to guide identification of in vitro substrates
title_fullStr Evaluation of Jumonji C lysine demethylase substrate preference to guide identification of in vitro substrates
title_full_unstemmed Evaluation of Jumonji C lysine demethylase substrate preference to guide identification of in vitro substrates
title_short Evaluation of Jumonji C lysine demethylase substrate preference to guide identification of in vitro substrates
title_sort evaluation of jumonji c lysine demethylase substrate preference to guide identification of in vitro substrates
topic Protocol
url 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
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