Abstract
Mass spectrometry has made major contributions to recent discoveries in the field of epigenetics, particularly in the characterization of the myriad post-translational modifications (PTMs) of histones which are technically challenging to analyze. These new developments have further aroused great interest in development of robust, new mass spectrometric methods to quantitatively study the dynamics of histone modifications. This review covers quantitative analysis of histone PTMs and discuss an ¹⁵N metabolic labeling procedure for quantifying histone PTMs applied to the analysis of methyltransferase knockouts in the model organism, Tetrahymena thermophila.
Copyright © 2013 Elsevier Inc. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Acetylation
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Amino Acid Sequence
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Gene Expression
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Histones / genetics
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Histones / isolation & purification*
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Histones / metabolism
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Humans
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Isotope Labeling
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Mass Spectrometry
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Methylation
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Molecular Sequence Data
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Nitrogen Isotopes
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Peptides / chemistry
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Peptides / isolation & purification*
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Protein Processing, Post-Translational*
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Tetrahymena thermophila / genetics
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Tetrahymena thermophila / metabolism*
Substances
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Histones
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Nitrogen Isotopes
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Peptides
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Recombinant Proteins