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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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3T3 Cells
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Acetyl Coenzyme A
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Acetylation
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Acetyltransferases / analysis*
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Acetyltransferases / isolation & purification
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Acetyltransferases / metabolism
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Amino Acid Sequence
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Animals
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Biotin
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Carbon Radioisotopes
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Histone Acetyltransferases
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Histones / chemistry
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Histones / genetics
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Mice
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Molecular Sequence Data
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Saccharomyces cerevisiae Proteins*
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Sensitivity and Specificity
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Streptavidin
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Substrate Specificity
Substances
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Carbon Radioisotopes
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Histones
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Peptide Fragments
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Recombinant Fusion Proteins
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Saccharomyces cerevisiae Proteins
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Biotin
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Acetyl Coenzyme A
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Streptavidin
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Acetyltransferases
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Histone Acetyltransferases