Mass Spectrometric Analysis of Histone Proteoforms
Open accessAbstract
Histones play important roles in chromatin, in the forms of various posttranslational modifications (PTMs) and sequence variants, which are called histone proteoforms. Investigating modifications and variants is an ongoing challenge. Previous methods are based on antibodies, and because they usually detect only one modification at a time, they are not suitable for studying the various combinations of modifications on histones. Fortunately, mass spectrometry (MS) has emerged as a high-throughput technology for histone analysis and does not require prior knowledge about any modifications. From the data generated by mass spectrometers, both identification and quantification of modifications, as well as variants, can be obtained easily. On the basis of this information, the functions of histones in various cellular contexts can be revealed. Therefore, MS continues to play an important role in the study of histone proteoforms. In this review, we discuss the analysis strategies of MS, their applications on histones, and some key remaining challenges.
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Histone proteoform analysis by Garcia and coworkers found far fewer histone proteoform variants than the maximal combinatorial possibilities would suggest.
“Garcia and coworkers have pioneered MS methods for histone proteoform analysis, finding much smaller numbers of histone proteoform variants than the maximal number of combinatorial possibilities would suggest (13).”
From Proteoforms as the next proteomics currency (2018) · cites this paper as [13]
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References 68 · Cited by 64
- Authors
- Yuan, Z.-F., Arnaudo, A. M., & Garcia, B. A.
- Affiliations
- University of Pennsylvania (US)
- Princeton University (US)
- Venue
- Annual Review of Analytical Chemistry
- Publisher
- Annual Reviews
- Published
- 2014-06-12
- Volume
- 7
- Issue
- 1
- Pages
- 113-128
- ISSN
- 1936-1327 (ISSN-L)
- 1936-1335
- PMC
- PMC4130481
- OpenAlex
- W2105971796
- Cited by
- 64
- References
- 68
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 1 · 2023: 3 · 2022: 2 · 2021: 6 · 2020: 10 · 2019: 8 · 2018: 7 · 2017: 1 · 2016: 9 · 2015: 9
- FWCI
- 0.62
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Annual Review of Analytical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation (CAREER)
- National Institutes of Health (DP2OD007447)
- 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 modifications, chromatin
- MeSH terms
- Animals, Chromatin, Histones, Humans, Protein Processing, Post-Translational, Mass Spectrometry
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