The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Identification of Combinatorial Patterns of Post-Translational Modifications on Individual Histones in the Mouse Brain
Open accessAbstract
Post-translational modifications (PTMs) of proteins are biochemical processes required for cellular functions and signalling that occur in every sub-cellular compartment. Multiple protein PTMs exist, and are established by specific enzymes that can act in basal conditions and upon cellular activity. In the nucleus, histone proteins are subjected to numerous PTMs that together form a histone code that contributes to regulate transcriptional activity and gene expression. Despite their importance however, histone PTMs have remained poorly characterised in most tissues, in particular the brain where they are thought to be required for complex functions such as learning and memory formation. Here, we report the comprehensive identification of histone PTMs, of their combinatorial patterns, and of the rules that govern these patterns in the adult mouse brain. Based on liquid chromatography, electron transfer, and collision-induced dissociation mass spectrometry, we generated a dataset containing a total of 10,646 peptides from H1, H2A, H2B, H3, H4, and variants in the adult brain. 1475 of these peptides carried one or more PTMs, including 141 unique sites and a total of 58 novel sites not described before. We observed that these PTMs are not only classical modifications such as serine/threonine (Ser/Thr) phosphorylation, lysine (Lys) acetylation, and Lys/arginine (Arg) methylation, but also include several atypical modifications such as Ser/Thr acetylation, and Lys butyrylation, crotonylation, and propionylation. Using synthetic peptides, we validated the presence of these atypical novel PTMs in the mouse brain. The application of data-mining algorithms further revealed that histone PTMs occur in specific combinations with different ratios. Overall, the present data newly identify a specific histone code in the mouse brain and reveal its level of complexity, suggesting its potential relevance for higher-order brain functions.
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Cites
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Lysine acetylation targets protein complexes and co-regulates major cellular functions
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ResultPeptide and protein sequence analysis by electron transfer dissociation mass spectrometry
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Cited by
Interpreting the language of histone and DNA modifications
Rothbart, S. B., & Strahl, B. D. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.03.001 · Cited by 720
Histone acetylation: molecular mnemonics on the chromatin
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Neural Mechanisms of Stress Resilience and Vulnerability
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Self-citationQuantitative Proteomic Analysis of Histone Modifications
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Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics
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Metadata
- Authors
- Tweedie-Cullen, R. Y., Brunner, A. M., Grossmann, J., Mohanna, S., Sichau, D., Nanni, P., Panse, C., & Mansuy, I. M.
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2012-05-31
- Volume
- 7
- Issue
- 5
- Pages
- e36980
- ISSN
- 1932-6203 (ISSN-L)
- OpenAlex
- W2059641703
- Cited by
- 163
- References
- 13
- FWCI
- 6.51
- Type
- journal article
- Language
- en
- Open access
- gold
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- Tweedie-Cullen, R. Y., Brunner, A. M., Grossmann, J., Mohanna, S., Sichau, D., Nanni, P., Panse, C., & Mansuy, I. M. (2012). Identification of Combinatorial Patterns of Post-Translational Modifications on Individual Histones in the Mouse Brain. PLoS ONE. https://doi.org/10.1371/journal.pone.0036980
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