Characterization of complete histone tail proteoforms using differential ion mobility spectrometry

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Authors
Shliaha, Pavel V.
Baird, Matthew A.
Nielsen, Mogens M.
Gorshkov, Vladimir A.
Bowman, Andrew P.
Kaszycki, Julia L.
Jensen, Ole N.
Shvartsburg, Alexandre A.
Issue Date
2017-05-16
Type
Article
Language
en_US
Keywords
Electron-transfer dissociation , Embryonic stem-cells , Mass-spectrometry , Posttranslational modifications , Faims-ms , Proteomics , Protein , Separation , Ionization , Phosphopeptides
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Abstract

Histone proteins are subject to dynamic post-translational modifications (PTMs) that cooperatively modulate the chromatin structure and function. Nearly all functional PTMs are found on the N-terminal histone domains (tails) of similar to 50 residues protruding from the nucleosome core. Using high-definition differential ion mobility spectrometry (FAIMS) with electron transfer dissociation, we demonstrate rapid baseline gas-phase separation and identification of tails involving rnonomethylation, trimethylation, acetylation, or phosphorylation in biologically relevant positions. These are by far the largest variant peptides resolved by any method, some with PTM contributing just 0.25% to the mass. This opens the door to similar separations for intact proteins and in top-down proteomics.

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ACS AuthorChoice - This is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
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Pavel V. Shliaha, Matthew A. Baird, Mogens M. Nielsen, Vladimir Gorshkov, Andrew P. Bowman, Julia L. Kaszycki, Ole N. Jensen, and Alexandre A. Characterization of complete histone tail proteoforms using differential ion mobility spectrometry. Analytical Chemistry 2017 89 (10), 5461-5466
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American Chemical Society
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0003-2700
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