Fluorogenic probes for detecting deacylase and demethylase activity towards post-translationally-modified lysine residues

Yuichiro Hori; Miyako Nishiura; Tomomi Tao; Reisuke Baba; Steven D. Bull; Kazuya Kikuchi

doi:10.1039/d0sc06551j

Fluorogenic probes for detecting deacylase and demethylase activity towards post-translationally-modified lysine residues

Yuichiro Hori, Miyako Nishiura, Tomomi Tao, Reisuke Baba, Steven D. Bull, Kazuya Kikuchi

Department of Chemistry

Osaka University

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

6 Citations (SciVal)

Abstract

Reversible enzymatic post-translational modification of the ε-amino groups of lysine residues (e.g. N-acylation reactions) plays an important role in regulating the cellular activities of numerous proteins. This study describes how enzyme catalyzed N-deprotection of lysine residues of non-fluorescent peptide-coumarin probes can be used to generate N-deprotected peptides that undergo spontaneousO- toN-ester transfer reactions (uncatalyzed) to generate a highly fluorescentN-carbamoyl peptide. This enables detection of enzyme catalyzedN-deacetylation,N-demalonylation,N-desuccinylation andN-demethylation reactions activities towards the N-modified lysine residues of these probes using simple ‘turn on’ fluorescent assays.

Original language	English
Pages (from-to)	2498-2503
Number of pages	6
Journal	Chemical Science
Volume	12
Issue number	7
Early online date	7 Feb 2021
DOIs	https://doi.org/10.1039/d0sc06551j
Publication status	Published - 21 Feb 2021

Bibliographical note

Funding Information:
This research was supported by JSPS KAKENHI (Grant Numbers JP19K22255, JP18H03935, JP17H06409 ?Frontier Research on Chemical Communications? to K. K. and JP17H02210, JP18K19402, JP20H02879 to Y. H.), JSPS A3 Foresight Program, JSPS Asian CORE Program, ?Asian Chemical Biology Initiative?, Japan (JSPS)-UK (RSC) Research Cooperative Program (JPJSBP120195705 to K. K.), Toray Science Foundation (19-6008) and Royal Society International Exchange (IEC\R3\183068 to S. D. Bull).

Publisher Copyright:
© The Royal Society of Chemistry 2021.

Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.

Funding

This research was supported by JSPS KAKENHI (Grant Numbers JP19K22255, JP18H03935, JP17H06409 ?Frontier Research on Chemical Communications? to K. K. and JP17H02210, JP18K19402, JP20H02879 to Y. H.), JSPS A3 Foresight Program, JSPS Asian CORE Program, ?Asian Chemical Biology Initiative?, Japan (JSPS)-UK (RSC) Research Cooperative Program (JPJSBP120195705 to K. K.), Toray Science Foundation (19-6008) and Royal Society International Exchange (IEC\R3\183068 to S. D. Bull).

ASJC Scopus subject areas

General Chemistry

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Cite this

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title = "Fluorogenic probes for detecting deacylase and demethylase activity towards post-translationally-modified lysine residues",

abstract = "Reversible enzymatic post-translational modification of the ε-amino groups of lysine residues (e.g. N-acylation reactions) plays an important role in regulating the cellular activities of numerous proteins. This study describes how enzyme catalyzed N-deprotection of lysine residues of non-fluorescent peptide-coumarin probes can be used to generate N-deprotected peptides that undergo spontaneousO- toN-ester transfer reactions (uncatalyzed) to generate a highly fluorescentN-carbamoyl peptide. This enables detection of enzyme catalyzedN-deacetylation,N-demalonylation,N-desuccinylation andN-demethylation reactions activities towards the N-modified lysine residues of these probes using simple {\textquoteleft}turn on{\textquoteright} fluorescent assays.",

author = "Yuichiro Hori and Miyako Nishiura and Tomomi Tao and Reisuke Baba and Bull, {Steven D.} and Kazuya Kikuchi",

note = "Funding Information: This research was supported by JSPS KAKENHI (Grant Numbers JP19K22255, JP18H03935, JP17H06409 ?Frontier Research on Chemical Communications? to K. K. and JP17H02210, JP18K19402, JP20H02879 to Y. H.), JSPS A3 Foresight Program, JSPS Asian CORE Program, ?Asian Chemical Biology Initiative?, Japan (JSPS)-UK (RSC) Research Cooperative Program (JPJSBP120195705 to K. K.), Toray Science Foundation (19-6008) and Royal Society International Exchange (IEC\R3\183068 to S. D. Bull). Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2021. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.",

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doi = "10.1039/d0sc06551j",

language = "English",

volume = "12",

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AU - Hori, Yuichiro

AU - Nishiura, Miyako

AU - Tao, Tomomi

AU - Baba, Reisuke

AU - Bull, Steven D.

AU - Kikuchi, Kazuya

N1 - Funding Information: This research was supported by JSPS KAKENHI (Grant Numbers JP19K22255, JP18H03935, JP17H06409 ?Frontier Research on Chemical Communications? to K. K. and JP17H02210, JP18K19402, JP20H02879 to Y. H.), JSPS A3 Foresight Program, JSPS Asian CORE Program, ?Asian Chemical Biology Initiative?, Japan (JSPS)-UK (RSC) Research Cooperative Program (JPJSBP120195705 to K. K.), Toray Science Foundation (19-6008) and Royal Society International Exchange (IEC\R3\183068 to S. D. Bull). Publisher Copyright: © The Royal Society of Chemistry 2021. Copyright: Copyright 2021 Elsevier B.V., All rights reserved.

PY - 2021/2/21

Y1 - 2021/2/21

N2 - Reversible enzymatic post-translational modification of the ε-amino groups of lysine residues (e.g. N-acylation reactions) plays an important role in regulating the cellular activities of numerous proteins. This study describes how enzyme catalyzed N-deprotection of lysine residues of non-fluorescent peptide-coumarin probes can be used to generate N-deprotected peptides that undergo spontaneousO- toN-ester transfer reactions (uncatalyzed) to generate a highly fluorescentN-carbamoyl peptide. This enables detection of enzyme catalyzedN-deacetylation,N-demalonylation,N-desuccinylation andN-demethylation reactions activities towards the N-modified lysine residues of these probes using simple ‘turn on’ fluorescent assays.

AB - Reversible enzymatic post-translational modification of the ε-amino groups of lysine residues (e.g. N-acylation reactions) plays an important role in regulating the cellular activities of numerous proteins. This study describes how enzyme catalyzed N-deprotection of lysine residues of non-fluorescent peptide-coumarin probes can be used to generate N-deprotected peptides that undergo spontaneousO- toN-ester transfer reactions (uncatalyzed) to generate a highly fluorescentN-carbamoyl peptide. This enables detection of enzyme catalyzedN-deacetylation,N-demalonylation,N-desuccinylation andN-demethylation reactions activities towards the N-modified lysine residues of these probes using simple ‘turn on’ fluorescent assays.

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Fluorogenic probes for detecting deacylase and demethylase activity towards post-translationally-modified lysine residues

Abstract

Bibliographical note

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