Mass spectrometry histones

Phanstiel, D. et al. (2008) Mass spectrometry identifies and quantifies 74 unique histone H4 isoforms in differentiating human embryonic stem cells. Proceedings of the National Academy of Sciences of the United States of America, 105, 4093 098. 

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... 

Aguilar, C., Hofte, A.J., Tjaden, U.R. and van der Greef, J. (2001) Analysis of histones by on-line capillary zone electrophoresis-electrospray ionisation mass spectrometry. Journal of Chromatography. A, 926, 57-67. 

Freitas, M.A., Sklenar, A.R. and Parthun, M.R. (2004) Application of mass spectrometry to the identification and quantification of histone post-translational modifications. Journal of Cellular Biochemistry, 92, 691—700. 

Zhang, L., Freitas, MA., Wickham, J., Parthun, M.R., Klisovic, M.I., Marcucd, G. and Byrd, J.C. (2004) Differential expression of histone post-translational modifications in acute myeloid and chronic lymphocytic leukemia determined by high-pressure liquid chromatography and mass spectrometry. Journal of the American Society for Mass Spectrometry, 15, 77-86. 

Yau, P.M. and Burlingame, A.L. (2002) Identification of acetylation and methylation sites of histone H3 from chicken erythrocytes by high-accuracy matrix-assisted laser desorption ionization-time-of-flight, matrix-assisted laser desorption ionization-postsource decay, and nanoelectrospray ionization tandem mass spectrometry. Analytical Biochemistry, 306, 259-269. 

Zhang, K Yau, P.M., Chandrasekhar, B New, R Kondrat, R Imai, B.S. and Bradbury, M.E. (2004) Differentiation between peptides containing acetylated or tri-methylated lysines by mass spectrometry an application for determining lysine 9 acetylation and methylation of histone H3. Proteomics,... 

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. 

Pesavento, J.J. Mizzen, C.A. Kelleher, N.L. Quantitative analysis of modified proteins and their positional isomers by tandem mass spectrometry Human histone H4. Anal. Chem. 2006, 78(13), 4271 280. 

Jung, H.R. Liu, W. Jensen, O.N. Determination of post-translational modifications of Histone H3 using chromatography, ion mobility tandem mass spectrometry and customized bioinformatics tools. Proc. 56th ASMS Conference on Mass Spectrometry and Allied Topics, Denver, CO, June 1-5, 2008, MP 394. 

F. 10 Schematic representation for the photo-affinity-based ABPP strategy. The structure of HDAC photo-crosslinking probe (SAHA-BPyne) is shown in the middle [115]. ABPP activity-based protein profiling, HDAC histone deacetylase, SAHA suberoylanilide hydroxamic acid, CuAAC copper(l)-catalyzed azide-alkyne cycloaddition, LC-MS/MS liquid chromatography-tandem mass spectrometry... 

Pesavento, j. J. Kim, Y. B. Taylor, G. K. Kelleher, N. L. Shotgun annotation of histone modifications A new approach for streamlined characterization of proteins by top down mass spectrometry. J. Am Chem. 

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