Mass spectrometry analysis of histone post translational modifications

Histone proteins play a central role in the dynamic structure of chromatin within the cell nucleus. The post translational modifications of histones can perturb chromatin contacts and the recruitment of non-histone proteins to chromatin. Alterations in the chromatin structure in which DNA is packaged influences the assembly of enzyme complexes that subsequently manipulate DNA. Therefore, such modifications may affect a wide range of biological processes which are potentially epigenetically inherited. The nature of histone marks and their importance in the epigenetic regulation of cellular functions has made them a prime candidate for study in both disease and drug discovery. The development of analytical tools that enable the identification and quantification of histone post translational modifications is therefore of significant interest. Mass spectrometry is a powerful tool for the global, unbiased, quantitative analysis of histone post translational modifications. Mass spectrometry allows the combinatorial nature of histone post translational modifications to be explored and has revolutionised the ability to study the histone code.

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