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Label-Free Relative Quantitation of Isobaric and Isomeric Human Histone H2A and H2B Variants by Fourier Transform Ion Cyclotron Resonance Top-Down MS/MS.

Title: Label-Free Relative Quantitation of Isobaric and Isomeric Human Histone H2A and H2B Variants by Fourier Transform Ion Cyclotron Resonance Top-Down MS/MS.
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Name(s): Dang, Xibei, author
Singh, Amar, author
Spetman, Brian D, author
Nolan, Krystal D, author
Isaacs, Jennifer S, author
Dennis, Jonathan H, author
Dalton, Stephen, author
Marshall, Alan G, author
Young, Nicolas L, author
Type of Resource: text
Genre: Journal Article
Text
Date Issued: 2016-09-02
Physical Form: computer
online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: Histone variants are known to play a central role in genome regulation and maintenance. However, many variants are inaccessible by antibody-based methods or bottom-up tandem mass spectrometry due to their highly similar sequences. For many, the only tractable approach is with intact protein top-down tandem mass spectrometry. Here, ultra-high-resolution FT-ICR MS and MS/MS yield quantitative relative abundances of all detected HeLa H2A and H2B isobaric and isomeric variants with a label-free approach. We extend the analysis to identify and relatively quantitate 16 proteoforms from 12 sequence variants of histone H2A and 10 proteoforms of histone H2B from three other cell lines: human embryonic stem cells (WA09), U937, and a prostate cancer cell line LaZ. The top-down MS/MS approach provides a path forward for more extensive elucidation of the biological role of many previously unstudied histone variants and post-translational modifications.
Identifier: FSU_pmch_27431976 (IID), 10.1021/acs.jproteome.6b00414 (DOI), PMC6261780 (PMCID), 27431976 (RID), 27431976 (EID)
Keywords: FT-ICR, FTMS, Histone, Post-translational modification, Proteoform, Sequence variants
Grant Number: P01 GM085354
Publication Note: This NIH-funded author manuscript originally appeared in PubMed Central at https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6261780.
Subject(s): Cell Line
Cyclotrons
Genetic Variation
Genomic Structural Variation
Histones/analysis
Histones/genetics
Humans
Protein Processing, Post-Translational
Proteomics/methods
Tandem Mass Spectrometry/methods
Persistent Link to This Record: http://purl.flvc.org/fsu/fd/FSU_pmch_27431976
Owner Institution: FSU
Is Part Of: Journal of proteome research.
1535-3907
Issue: iss. 9, vol. 15

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Dang, X., Singh, A., Spetman, B. D., Nolan, K. D., Isaacs, J. S., Dennis, J. H., … Young, N. L. (2016). Label-Free Relative Quantitation of Isobaric and Isomeric Human Histone H2A and H2B Variants by Fourier Transform Ion Cyclotron Resonance Top-Down MS/MS. Journal Of Proteome Research. Retrieved from http://purl.flvc.org/fsu/fd/FSU_pmch_27431976