A rapid and sensitive assay for histone acetyl-transferase activity

S. Ait-Si-Ali; S. Ramirez; P. Robin; D. Trouche; A. Harel-Bellan

doi:10.1093/nar/26.16.3869

A rapid and sensitive assay for histone acetyl-transferase activity

S. Ait-Si-Ali
, S. Ramirez
, P. Robin
, D. Trouche
, A. Harel-Bellan

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

52 Scopus citations

Abstract

Histone acetyl-transferases (HATs) seem to be key elements in the regulation of transcription. We have designed an enzymatic assay to quantify HAT enzymatic activity. In this assay, the substrate is a peptide corresponding to the 24 first amino acids of histone H4 which is coupled to biotin. After acetylation using [¹⁴C]acetyl-CoA, the peptide is purified on streptavidin beads and the associated radioactivity is measured. This assay is sensitive, rapid and convenient.

Original language	English (US)
Pages (from-to)	3869-3870
Number of pages	2
Journal	Nucleic Acids Research
Volume	26
Issue number	16
DOIs	https://doi.org/10.1093/nar/26.16.3869
State	Published - Aug 15 1998
Externally published	Yes

All Science Journal Classification (ASJC) codes

Genetics

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10.1093/nar/26.16.3869

Cite this

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title = "A rapid and sensitive assay for histone acetyl-transferase activity",

abstract = "Histone acetyl-transferases (HATs) seem to be key elements in the regulation of transcription. We have designed an enzymatic assay to quantify HAT enzymatic activity. In this assay, the substrate is a peptide corresponding to the 24 first amino acids of histone H4 which is coupled to biotin. After acetylation using [14C]acetyl-CoA, the peptide is purified on streptavidin beads and the associated radioactivity is measured. This assay is sensitive, rapid and convenient.",

author = "S. Ait-Si-Ali and S. Ramirez and P. Robin and D. Trouche and A. Harel-Bellan",

note = "Funding Information: This work was supported by grants from the Ligue Nationale contre le Cancer, the Comit{\'e} de l{\textquoteright}Essone, the Comit{\'e} du Val de Marne, the Comit{\'e} des Yvelines of the Ligue Nationale contre le Cancer and from the Association pour la Recherche sur le Cancer. S.A. was a recipient of a fellowship from the Comit{\'e} de la Haute-Sa{\^o}ne of the Ligue Nationale contre le Cancer. S.R. was a recipient of a travel award from the Colombian Government (Colcencias). The authors wish to thank Chiron for their help in the design and the synthesis of the peptide and Linda L. Pritchard for critical reading of the manuscript.",

year = "1998",

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doi = "10.1093/nar/26.16.3869",

language = "English (US)",

volume = "26",

pages = "3869--3870",

journal = "Nucleic Acids Research",

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TY - JOUR

T1 - A rapid and sensitive assay for histone acetyl-transferase activity

AU - Ait-Si-Ali, S.

AU - Ramirez, S.

AU - Robin, P.

AU - Trouche, D.

AU - Harel-Bellan, A.

N1 - Funding Information: This work was supported by grants from the Ligue Nationale contre le Cancer, the Comité de l’Essone, the Comité du Val de Marne, the Comité des Yvelines of the Ligue Nationale contre le Cancer and from the Association pour la Recherche sur le Cancer. S.A. was a recipient of a fellowship from the Comité de la Haute-Saône of the Ligue Nationale contre le Cancer. S.R. was a recipient of a travel award from the Colombian Government (Colcencias). The authors wish to thank Chiron for their help in the design and the synthesis of the peptide and Linda L. Pritchard for critical reading of the manuscript.

PY - 1998/8/15

Y1 - 1998/8/15

N2 - Histone acetyl-transferases (HATs) seem to be key elements in the regulation of transcription. We have designed an enzymatic assay to quantify HAT enzymatic activity. In this assay, the substrate is a peptide corresponding to the 24 first amino acids of histone H4 which is coupled to biotin. After acetylation using [14C]acetyl-CoA, the peptide is purified on streptavidin beads and the associated radioactivity is measured. This assay is sensitive, rapid and convenient.

AB - Histone acetyl-transferases (HATs) seem to be key elements in the regulation of transcription. We have designed an enzymatic assay to quantify HAT enzymatic activity. In this assay, the substrate is a peptide corresponding to the 24 first amino acids of histone H4 which is coupled to biotin. After acetylation using [14C]acetyl-CoA, the peptide is purified on streptavidin beads and the associated radioactivity is measured. This assay is sensitive, rapid and convenient.

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UR - https://www.scopus.com/pages/publications/0032529482#tab=citedBy

U2 - 10.1093/nar/26.16.3869

DO - 10.1093/nar/26.16.3869

M3 - Research Article

C2 - 9685509

AN - SCOPUS:0032529482

SN - 0305-1048

VL - 26

SP - 3869

EP - 3870

JO - Nucleic Acids Research

JF - Nucleic Acids Research

IS - 16

ER -

A rapid and sensitive assay for histone acetyl-transferase activity

Abstract

All Science Journal Classification (ASJC) codes

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