Mass histone modification analysis

Histone Modification Analysis Using Mass Spectrometry... 

Mass spectrometry provides a more direct and precise technique to study histone modifications. As with the other methods discussed above, mass spectrometry also has several pitfalls that should be taken into account when analyzing histone modifications. First of all histones and especially the core histones H3 and H4 are rich in lysine residues. Consequently, trypsin as an enzyme that is routinely used for the identification of proteins via peptide mass fingerprints cannot be used for regular in gel digestion of histones. Other enzymes that have a different specificity (such as Asp-N or Arg-C) are more frequently used in the analysis of histones [25]. A drawback... 

Bonaldi, T., Imhof, A. and Regula, J.T. (2004) A combination of different mass spectroscopic techniques for the analysis of dynamic changes of histone modifications. Proteomics, 4, 1382—1396. 

Syka, J. E. P. Marto, J. A. Bai, D. L. Homing, S. Senko, M. W Schwartz, J. C. Ueberheide, B. Garcia, B. Busby, S. Muratore, T Shabanowitz, J. Hunt, D. F. Novel linear quadmpole ion trap/FT mass spectrometer performance characterization and use in the comparative analysis of histone H3 post-translational modifications. 

Johnson, L., Mollah, S., Garcia, B. A., Muratore, T. F., Shabanowitz, J., Hunt, D. F., and Jacobsen, S. E. (2004). Mass spectrometry analysis of Arabidopsis histone H3 reveals distinct combinations of post-translational modifications. Nucleic Acids Res. 32 6511 -6518. 

Syka JEP, Marto JA, Bai DL, Homing S, Senko MW, Schwartz JC, Ueberheide B, Garcia B, Busby S, Muratore T, Shabanowitz J, Hunt DF. Novel linear quadrapole ion trap/FT mass spectrometer Performance characterization and use in the comparative analysis of histone H3 post-translational modifications. J Proteome Res 2004 3(3) 621-626. 

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