Characterization of Complete Histone Tail Proteoforms Using Differential Ion Mobility Spectrometry

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 ∼50 residues protruding from the nucleosome core. Using high-definition...

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Published inAnalytical chemistry (Washington) Vol. 89; no. 10; pp. 5461 - 5466
Main Authors Shliaha, Pavel V, Baird, Matthew A, Nielsen, Mogens M, Gorshkov, Vladimir, Bowman, Andrew P, Kaszycki, Julia L, Jensen, Ole N, Shvartsburg, Alexandre A
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 16.05.2017
Subjects
Acetylation
Analytical chemistry
Chemistry
Chromatin
dissociation
Electron transfer
Functional anatomy
gases
histones
Ionic mobility
Methylation
Mobility
nucleosomes
Peptides
Phase separation
Phosphorylation
Post-translation
post-translational modification
Proteins
Proteomics
Residues
Spectrometry
Spectroscopy
Structure-function relationships
Translation
Online AccessGet full text
ISSN0003-2700
1520-6882
1520-6882
DOI10.1021/acs.analchem.7b00379

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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 ∼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 monomethylation, 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.
AbstractList 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 ~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 monomethylation, 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.
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 ∼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 monomethylation, 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.
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 ∼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 monomethylation, 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.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 ∼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 monomethylation, 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.
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 ∼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 monomethylation, 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.
Author Nielsen, Mogens M
Gorshkov, Vladimir
Baird, Matthew A
Bowman, Andrew P
Jensen, Ole N
Shvartsburg, Alexandre A
Shliaha, Pavel V
Kaszycki, Julia L
AuthorAffiliation Department of Chemistry
University of Southern Denmark
Department of Biochemistry and Molecular Biology, VILLUM Center for Bioanalytical Sciences, and Center for Epigenetics
Wichita State University
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  organization: University of Southern Denmark
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  orcidid: 0000-0003-0170-5785
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Snippet Histone proteins are subject to dynamic post-translational modifications (PTMs) that cooperatively modulate the chromatin structure and function. Nearly all...
Histone proteins are subject to dynamic post-translational modifications (PTMs) that cooperatively modulate the chromatin structure and function. Nearly all...
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StartPage 5461
SubjectTerms Acetylation
Analytical chemistry
Chemistry
Chromatin
dissociation
Electron transfer
Functional anatomy
gases
histones
Ionic mobility
Methylation
Mobility
nucleosomes
Peptides
Phase separation
Phosphorylation
Post-translation
post-translational modification
Proteins
Proteomics
Residues
Spectrometry
Spectroscopy
Structure-function relationships
Translation
Title Characterization of Complete Histone Tail Proteoforms Using Differential Ion Mobility Spectrometry
URI http://dx.doi.org/10.1021/acs.analchem.7b00379
https://www.ncbi.nlm.nih.gov/pubmed/28406606
https://www.proquest.com/docview/1908341409
https://www.proquest.com/docview/1888681061
https://www.proquest.com/docview/2000345229
https://pubmed.ncbi.nlm.nih.gov/PMC5436587
Volume 89
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