Methyl group migration during the fragmentation of singly charged ions of trimethyllysine-containing peptides: Precaution of using MS/MS of singly charged ions for interrogating peptide methylation |
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Authors: | Lei Xiong Liyan Ping Bifeng Yuan Yinsheng Wang |
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Institution: | 1. Department of Chemistry-027, University of California at Riverdale, 900 University Avenue, 92521-0403, Riverdale, CA, USA
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Abstract: | Core histones are susceptible to a range of post-translational modifications (PTMs), including acetylation, phosphorylation,
methylation, and ubiquitination, which play important roles in the epigenetic control of gene expression. Here, we observed
an unusual discrepancy between MALDI-MS/MS and ESI-MS/MS on the methylation of trimethyllysine-containing peptides with residues
9–17 from human histone H3 and residues 73–83 from yeast histone H3. It turned out that the discrepancy could be attributed
to an unusual methyl group migration from the side chain of trimethyllysine to the C-terminal arginine residue during peptide
fragmentation, and this methyl group transfer only occurred for singly charged ions, but not for doubly charged ions. The
methyl group transfer argument received its support from the results on the studies of the fragmentation of the ESI- or MALDI-produced
singly charged ions of several synthetic trimethyllysine-bearing peptides. The results presented in this study highlighted
that caution should be exerted while MS/MS of singly charged ions is employed to interrogate the PTMs of trimethyllysine-containing
peptides. |
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