Label-Free Relative Quantitation of Isobaric and Isomeric Human Histone H2A and H2B Variants by Fourier Transform Ion Cyclotron Resonance Top-Down MS/MS
Open accessAbstract
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.
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In cancer epigenetics, there are several examples in which PTM crosstalk has been mapped definitively.
“In cancer epigenetics, there are several examples in which PTM crosstalk has been mapped definitively (see also the top rows of Table 1) 22,45-49 .”
From How many human proteoforms are there? (2018) · cites this paper as [46]
The Results and Discussion section reports identifying and quantifying histone proteoforms in a prostate cancer cell line, but does not describe definitively mapped PTM crosstalk. Searches for “crosstalk” and for interactions or co-occurrence of modifications in cancer found no passage addressing that claim; the cited paper instead presents its method as a path toward further study. (LLM, conf=0.74)
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Cites
Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756 · see citing works
Regulation of chromatin by histone modifications
Bannister, A. J., & Kouzarides, T. (2011) · Cell Research · doi:10.1038/cr.2011.22 · Cited by 6,012 · see citing works
Chen, X., Xiu, M., Xing, J., Yu, S., Min, D., & Guo, F. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479439 · Cited by 5,759 · see citing works
Stability and flexibility of epigenetic gene regulation in mammalian development
Reik, W. (2007) · Nature · doi:10.1038/nature05918 · Cited by 1,963 · see citing works
Proteoform: a single term describing protein complexity
The Consortium for Top Down Proteomics, Smith, L. M., & Kelleher, N. L. (2013) · Nature Methods · doi:10.1038/nmeth.2369 · Cited by 1,528 · see citing works
Histone modifications in transcriptional regulation
Berger, S. L. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00279-4 · Cited by 1,222 · see citing works
Regulation of HP1–chromatin binding by histone H3 methylation and phosphorylation
Fischle, W., Tseng, B. S., Dormann, H. L., Ueberheide, B. M., Garcia, B. A., Shabanowitz, J., Hunt, D. F., Funabiki, H., & Allis, C. D. (2005) · Nature · doi:10.1038/nature04219 · Cited by 996 · see citing works
Chromatin Challenges during DNA Replication and Repair
Groth, A., Rocha, W., Verreault, A., & Almouzni, G. (2007) · Cell · doi:10.1016/j.cell.2007.01.030 · Cited by 733 · see citing works
Kinetics of Core Histones in Living Human Cells
Kimura, H., & Cook, P. R. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.7.1341 · Cited by 675 · see citing works
Top Down proteomics: Facts and perspectives
Catherman, A. D., Skinner, O. S., & Kelleher, N. L. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.02.041 · Cited by 507 · see citing works
Space charge effects in Fourier transform mass spectrometry. II. Mass calibration
Ledford, E. B., Rempel, D. L., & Gross, M. L. (1984) · Analytical Chemistry · doi:10.1021/ac00278a027 · Cited by 469 · see citing works
Mass spectrometry-based proteomics: existing capabilities and future directions
Angel, T. E., Aryal, U. K., Hengel, S. M., Baker, E. S., Kelly, R., Robinson, E. W., & Smith, R. D. (2012) · Chemical Society Reviews · doi:10.1039/c2cs15331a · Cited by 443 · see citing works
Partitioning of Histone H3-H4 Tetramers During DNA Replication–Dependent Chromatin Assembly
Xu, M., Long, C., Chen, X., Huang, C., Chen, S., & Zhu, B. (2010) · Science · doi:10.1126/science.1178994 · Cited by 351 · see citing works
Maze, I. S., Noh, K., Soshnev, A. A., & Allis, C. D. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3673 · Cited by 347 · see citing works
Epigenetics—An Epicenter of Gene Regulation: Histones and Histone‐Modifying Enzymes
Biel, M., Wascholowski, V., & Giannis, A. (2005) · Angewandte Chemie International Edition · doi:10.1002/anie.200461346 · Cited by 321 · see citing works
Guan, S., & Marshall, A. G. (1996) · International Journal of Mass Spectrometry and Ion Processes · doi:10.1016/s0168-1176(96)04461-8 · Cited by 321 · see citing works
Self-citationHistone H2A variants in nucleosomes and chromatin: more or less stable?
Bönisch, C., & Hake, S. B. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks865 · Cited by 305 · see citing works
Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification
Tessarz, P., Santos-Rosa, H., Robson, S. C., Sylvestersen, K. B., Nelson, C. J., Nielsen, M. L., & Kouzarides, T. (2014) · Nature · doi:10.1038/nature12819 · Cited by 243 · see citing works
Androgen-repressed phenotype in human prostate cancer
Zhau, H. E., Chang, S., Chen, B.-Q., Wang, Y., Zhang, H., Kao, C. H., Sang, Q. A., Pathak, S. J., & Chung, L. W. K. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15152 · Cited by 231 · see citing works
A Novel 9.4 Tesla FTICR Mass Spectrometer with Improved Sensitivity, Mass Resolution, and Mass Range
Kaiser, N. K., Quinn, J. P., Blakney, G. T., Hendrickson, C. L., & Marshall, A. G. (2011) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-011-0141-9 · Cited by 225 · see citing works
Self-citationShi, S. D. ‐., Drader, J. J., Freitas, M. A., Hendrickson, C. L., & Marshall, A. G. (2000) · International Journal of Mass Spectrometry · doi:10.1016/s1387-3806(99)00226-2 · Cited by 181 · see citing works
Self-citationPrecise Characterization of Human Histones in the H2A Gene Family by Top Down Mass Spectrometry
Boyne, M. T., Pesavento, J. J., Mizzen, C. A., & Kelleher, N. L. (2006) · Journal of Proteome Research · doi:10.1021/pr050269n · Cited by 157 · see citing works
Hance, M. W., Dole, K., Gopal, U., Bohonowych, J. E. S., Jezierska‐Drutel, A., Neumann, C. A., Liu, H., Garraway, I. P., & Isaacs, J. S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.389015 · Cited by 147 · see citing works
Self-citationHistone Variants in Metazoan Development
Banaszynski, L. A., Allis, C. D., & Lewis, P. W. (2010) · Developmental Cell · doi:10.1016/j.devcel.2010.10.014 · Cited by 147 · see citing works
Singh, A. M., Chappell, J., Trost, R., Lin, L., Wang, T., Tang, J., Wu, H., Zhao, S., Jin, P., & Dalton, S. (2013) · Stem Cell Reports · doi:10.1016/j.stemcr.2013.10.009 · Cited by 136 · see citing works
Self-citationSingh, A. M., Chappell, J., Trost, R., Lin, L., Wang, T., Tang, J., Matlock, B. K., Weller, K. P., Wu, H., Zhao, S., et al. (2014) · Stem Cell Reports · doi:10.1016/j.stemcr.2014.02.009 · Cited by 126 · see citing works
Self-citationThe activity-dependent histone variant H2BE modulates the life span of olfactory neurons
Santoro, S. W., & Dulac, C. G. (2012) · eLife · doi:10.7554/elife.00070 · Cited by 122 · see citing works
The first pilot project of the consortium for top‐down proteomics: A status report
Dang, X., Scotcher, J., Wu, S., Chu, R., Tolić, N., Ntai, I., Thomas, P. M., Fellers, R. T., Early, B. P., Zheng, Y., et al. (2014) · PROTEOMICS · doi:10.1002/pmic.201300438 · Cited by 101 · see citing works
Self-citationGene-specific characterization of human histone H2B by electron capture dissociation.
Siuti, N., Roth, M. J., Mizzen, C., Kelleher, N., & Pesavento, J. J. (2006) · Journal of Proteome Research · doi:10.1021/pr050268v · Cited by 101 · see citing works
H2B Tyr37 phosphorylation suppresses expression of replication-dependent core histone genes
Mahajan, K. N., Fang, B., Koomen, J. M., & Mahajan, N. P. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2356 · Cited by 96 · see citing works
Liu, C., Liu, L., Shan, J., Shen, J., Xu, Y., Zhang, Q., Yang, Z., Wu, L., Xia, F., Bie, P., et al. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.07.022 · Cited by 79 · see citing works
Tumor-secreted Hsp90 Subverts Polycomb Function to Drive Prostate Tumor Growth and Invasion
Nolan, K. D., Franco, O. E., Hance, M. W., Hayward, S. W., & Isaacs, J. S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.637496 · Cited by 78 · see citing works
Self-citationAnderson, L. C., Karch, K. R., Ugrin, S. A., Coradin, M., English, A. M., Sidoli, S., Shabanowitz, J., Garcia, B. A., & Hunt, D. F. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o115.053843 · Cited by 60 · see citing works
Phosphorylation of Histone H2A Inhibits Transcription on Chromatin Templates
Zhang, Y., Griffin, K., Mondal, N., & Parvin, J. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400099200 · Cited by 59 · see citing works
Multi-faceted quantitative proteomics analysis of histone H2B isoforms and their modifications
Molden, R. C., Bhanu, N. V., LeRoy, G., Arnaudo, A. M., & Garcia, B. A. (2015) · Epigenetics & Chromatin · doi:10.1186/s13072-015-0006-8 · Cited by 55 · see citing works
Kalli, A., Sweredoski, M. J., & Hess, S. Y. (2013) · Analytical Chemistry · doi:10.1021/ac303103b · Cited by 35 · see citing works
Human histone acetyltransferase 1 (Hat1) acetylates lysine 5 of histone H2A in vivo
Tafrova, J. I., & Tafrov, S. T. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-014-2036-0 · Cited by 24 · see citing works
Utilizing FUCCI reporters to understand pluripotent stem cell biology
Singh, A. M., Trost, R., Boward, B., & Dalton, S. (2015) · Methods · doi:10.1016/j.ymeth.2015.09.020 · Cited by 16 · see citing works
Self-citation
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Research works printed but not linked: 1
- [28]Anderson LC; He L; Marshall AG; Hendrickson CL Analysis of a Monoclonal Antibody by Top-Down LC-MS/MS with a 21 Tesla FT-ICR Mass Spectrometer, Sanibel Conference on Characterization of Protein Therapeutics by Mass Spectrometry, Hilton Clearwater Beach, Florida, 21-24 Jan, 2016.
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Brodbelt, J. S. (2015) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04563 · Cited by 245 · see citing works
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Chen, B., Brown, K. A., Lin, Z., & Ge, Y. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04747 · Cited by 210 · see citing works
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Riley, N. M., & Coon, J. J. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b04810 · Cited by 180 · see citing works
The punctilious RNA polymerase II core promoterPreprint
Ngoc, L. V., Wang, Y., Kassavetis, G. A., & Kadonaga, J. T. (2017) · Genes & Development · doi:10.1101/gad.303149.117 · Cited by 145 · see citing works
The Blood Proteoform Atlas: A reference map of proteoforms in human hematopoietic cells
Melani, R. D., Gerbasi, V. R., Anderson, L. C., Sikora, J. W., Toby, T. K., Hutton, J. E., Butcher, D. S., Negrão, F., Seckler, H. S., Srzentić, K., et al. (2022) · Science · doi:10.1126/science.aaz5284 · Cited by 140 · see citing works
Ion Activation Methods for Peptides and Proteins
Macias, L. A., Santos, I. C., & Brodbelt, J. S. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b04859 · Cited by 107 · see citing works
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Taylor, B. C., & Young, N. L. (2021) · Biochemical Journal · doi:10.1042/bcj20200170 · Cited by 93 · see citing works
Self-citationGargano, A. F. G., Shaw, J. B., Zhou, M., Wilkins, C. S., Fillmore, T. L., Moore, R. J., Somsen, G. W., & Paša-Tolić, L. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00458 · Cited by 53 · see citing works
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Holt, M. V., Wang, T., & Young, N. L. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02350-z · Cited by 48 · see citing works
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Joseph, F. M., & Young, N. L. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.012 · Cited by 43 · see citing works
Self-citationYu, D., Wang, Z., Cupp-Sutton, K. A., Liu, X., & Wu, S. (2019) · Journal of the American Society for Mass Spectrometry · doi:10.1007/s13361-019-02315-2 · Cited by 39 · see citing works
Chen, D., Yang, Z., Shen, X., & Sun, L. (2021) · Analytical Chemistry · doi:10.1021/acs.analchem.0c04237 · Cited by 35 · see citing works
Simithy, J., Sidoli, S., & Garcia, B. A. (2018) · PROTEOMICS · doi:10.1002/pmic.201700309 · Cited by 30 · see citing works
Ma, J., Dai, Q., Li, X., Zhu, X., Ma, T., Qiao, X., Shen, S., & Liu, X. (2017) · Analytica Chimica Acta · doi:10.1016/j.aca.2017.01.057 · Cited by 29 · see citing works
Khan, A., Eikani, C. K., Khan, H., Iavarone, A. T., & Pesavento, J. J. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00780 · Cited by 27 · see citing works
Rommelfanger, S. R., Zhou, M., Shaghasi, H., Tzeng, S., Evans, B. S., Paša‐Tolić, L., Umen, J., & Pesavento, J. J. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.1c00029 · Cited by 23 · see citing works
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- Authors
- Dang, X., Singh, A., Spetman, B. D., Nolan, K. D., Isaacs, J. S., Dennis, J. H., Dalton, S., Marshall, A. G., & Young, N. L.
- Affiliations
- Florida State University (US)
- University of Georgia (US)
- Medical University of South Carolina (US)
- Baylor College of Medicine (US)
- Corresponding author
- Young, Nicolas L.
- Venue
- Journal of Proteome Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2016-08-03
- Volume
- 15
- Issue
- 9
- Pages
- 3196-3203
- ISSN
- 1535-3893 (ISSN-L)
- 1535-3907
- PMC
- PMC6261780
- OpenAlex
- W2497408826
- Cited by
- 41
- References
- 38
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 5 · 2023: 2 · 2022: 4 · 2021: 7 · 2020: 2 · 2019: 3 · 2018: 4 · 2017: 6 · 2015: 1
- FWCI
- 2.16
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Proteome Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (P01GM85354)
- National Science Foundation (DMR-06-54118)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- histone variants, histone H2A, histone H2B, proteoforms, HeLa cells, human embryonic stem cells, U937 cells, prostate cancer cell lines, post-translational modification, histone modifications
- MeSH terms
- Cell Line, Histones, Humans, Protein Processing, Post-Translational, Genetic Variation, Cyclotrons, Proteomics, Tandem Mass Spectrometry, Genomic Structural Variation
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