Histones ubiquitylation

McGinty R.K., Kim, J., Chatterjee, C., Roeder, R.G. and Muir, T.W. (2008) Chemically ubiquitylated histone H2B stimulates hDotlL-mediated intranucleosomal methylation. Nature, 453, 812-816. 

Figure 5.3 Selected post-translational modifications of human histones. Methylation, acetylation, phosphorylation, biotinylation and ubiquitylation sites have been identified on all four core histones. The modifications shown here should not be regarded as a complete or final list.

Identification and characterization of the many different PTMs that DNA-binding proteins can be subject to is important to understand their functions and how these are controlled. The best-known examples of this are certainly the histones, which are subject to nearly all PTMs known for DNA-binding proteins including acetylation, methylation, phosphorylation, ADP-ribosylation, biotinylation, sumoylation, and ubiquitylation. For this reason the histones have been chosen as examples to illustrate the application of ESI and MALDI MS for the identification and characterization of PTMs. 

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