Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins

Richard C. Brewster; Georgina C. Gavins; Barbara Günthardt; Sarah Farr; Kimberly M. Webb; Philipp Voigt; Alison N. Hulme

doi:10.1039/C6CC06801D

Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins

Richard C. Brewster, Georgina C. Gavins, Barbara Günthardt, Sarah Farr, Kimberly M. Webb, Philipp Voigt, Alison N. Hulme

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

Abstract

Rapid, site-selective modification of cysteine residues with chloromethyl-triazole derivatives generates pseudo-acyl sLys motifs, mimicking important post-translational modifications. Near-native biotinylation of peptide and protein substrates is shown to be site-selective and modified histone H4 retains functional activity.

Original language	English
Pages (from-to)	12230-12232
Number of pages	3
Journal	Chemical Communications
Volume	52
Issue number	82
Early online date	13 Sept 2016
DOIs	https://doi.org/10.1039/C6CC06801D
Publication status	E-pub ahead of print - 13 Sept 2016

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10.1039/C6CC06801D

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Roles of symmetric and asymmetric histone H3 lysine 27 trimethylation in gene repression and epigenetic inheritance
Voigt, P. & Finnegan, D.
UK-based charities
1/11/14 → 31/12/21
Project: Research
Core funding renewal for the Wellcome Trust Centre for Cell Biology
Tollervey, D. & Earnshaw, B.
UK-based charities
1/10/11 → 30/04/17
Project: Research

Chloromethyl-triazole: A new motif for site-selective pseudo-acylation of proteins
Brewster, R. (Creator), Gavins, G. C. (Creator), Günthardt, B. (Creator), Farr, S. (Creator), Webb, K. M. (Creator), Voigt, P. (Creator) & Hulme, A. (Creator), Edinburgh DataShare, 16 Sept 2016
DOI: 10.7488/ds/1484
Dataset

Alison Hulme
- School of Chemistry - Personal Chair of Synthesis and Chemical Biology
- EaStCHEM
Person: Academic: Research Active

Cite this

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title = "Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins",

abstract = "Rapid, site-selective modification of cysteine residues with chloromethyl-triazole derivatives generates pseudo-acyl sLys motifs, mimicking important post-translational modifications. Near-native biotinylation of peptide and protein substrates is shown to be site-selective and modified histone H4 retains functional activity.",

author = "Brewster, {Richard C.} and Gavins, {Georgina C.} and Barbara G{\"u}nthardt and Sarah Farr and Webb, {Kimberly M.} and Philipp Voigt and Hulme, {Alison N.}",

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language = "English",

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AU - Günthardt, Barbara

AU - Farr, Sarah

AU - Webb, Kimberly M.

AU - Voigt, Philipp

AU - Hulme, Alison N.

PY - 2016/9/13

Y1 - 2016/9/13

N2 - Rapid, site-selective modification of cysteine residues with chloromethyl-triazole derivatives generates pseudo-acyl sLys motifs, mimicking important post-translational modifications. Near-native biotinylation of peptide and protein substrates is shown to be site-selective and modified histone H4 retains functional activity.

AB - Rapid, site-selective modification of cysteine residues with chloromethyl-triazole derivatives generates pseudo-acyl sLys motifs, mimicking important post-translational modifications. Near-native biotinylation of peptide and protein substrates is shown to be site-selective and modified histone H4 retains functional activity.

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DO - 10.1039/C6CC06801D

M3 - Article

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SP - 12230

EP - 12232

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Chloromethyl-triazole: a new motif for site-selective pseudo-acylation of proteins

Abstract

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Roles of symmetric and asymmetric histone H3 lysine 27 trimethylation in gene repression and epigenetic inheritance

Core funding renewal for the Wellcome Trust Centre for Cell Biology

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Chloromethyl-triazole: A new motif for site-selective pseudo-acylation of proteins

Profiles

Alison Hulme

Cite this