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

Matthew Hoekstra; Anand Chopra; William G. Willmore; Kyle K. Biggar

doi:10.1016/j.xpro.2022.101271

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

Matthew Hoekstra
, Anand Chopra
, William G. Willmore
, Kyle K. Biggar

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

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).

Original language	English
Article number	101271
Journal	STAR Protocols
Volume	3
Issue number	2
DOIs	https://doi.org/10.1016/j.xpro.2022.101271
State	Published - 17 Jun 2022
Externally published	Yes

Keywords

High Throughput Screening
Molecular Biology
Protein Biochemistry
Protein expression and purification
Systems biology

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology
General Neuroscience
General Immunology and Microbiology
General Medicine

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10.1016/j.xpro.2022.101271

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title = "Evaluation of Jumonji C lysine demethylase substrate preference to guide identification of in vitro substrates",

abstract = "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).",

keywords = "High Throughput Screening, Molecular Biology, Protein Biochemistry, Protein expression and purification, Systems biology",

author = "Matthew Hoekstra and Anand Chopra and Willmore, \{William G.\} and Biggar, \{Kyle K.\}",

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year = "2022",

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doi = "10.1016/j.xpro.2022.101271",

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TY - JOUR

T1 - Evaluation of Jumonji C lysine demethylase substrate preference to guide identification of in vitro substrates

AU - Hoekstra, Matthew

AU - Chopra, Anand

AU - Willmore, William G.

AU - Biggar, Kyle K.

PY - 2022/6/17

Y1 - 2022/6/17

N2 - 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).

AB - 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).

KW - High Throughput Screening

KW - Molecular Biology

KW - Protein Biochemistry

KW - Protein expression and purification

KW - Systems biology

UR - https://www.scopus.com/pages/publications/85127121740

U2 - 10.1016/j.xpro.2022.101271

DO - 10.1016/j.xpro.2022.101271

M3 - Article

C2 - 35378885

AN - SCOPUS:85127121740

SN - 2666-1667

VL - 3

JO - STAR Protocols

JF - STAR Protocols

IS - 2

M1 - 101271

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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