N ε -Formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function
Open accessAbstract
Post-translational modification of histones and other chromosomal proteins regulates chromatin conformation and gene activity. Methylation and acetylation of lysyl residues are among the most frequently described modifications in these proteins. Whereas these modifications have been studied in detail, very little is known about a recently discovered chemical modification, the N(epsilon)-lysine formylation, in histones and other nuclear proteins. Here we mapped, for the first time, the sites of lysine formylation in histones and several other nuclear proteins. We found that core and linker histones are formylated at multiple lysyl residues located both in the tails and globular domains of histones. In core histones, formylation was found at lysyl residues known to be involved in organization of nucleosomal particles that are frequently acetylated and methylated. In linker histones and high mobility group proteins, multiple formylation sites were mapped to residues with important role in DNA binding. N(epsilon)-lysine formylation in chromosomal proteins is relatively abundant, suggesting that it may interfere with epigenetic mechanisms governing chromatin function, which could lead to deregulation of the cell and disease.
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Large variety of novel histone marks, such as formylation, propionylation, butyrylation, malonylation, and succinylation, have been identified by tandem mass spectrometry.
“In fact, a large variety of novel histone marks, such as formylation, propionylation, butyrylation, malonylation and succinylation have recently been identified by tandem mass spectrometry (Chen et al., 2007; Wisniewski et al., 2008; Xie et al., 2012).”
From The emerging hallmarks of cancer metabolism (2016) · cites this paper as Wisniewski et al., 2008
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- Authors
- Wiśniewski, J. R., Zougman, A., & Mann, M.
- Affiliations
- Max Planck Society (DE)
- Corresponding author
- Wiśniewski, Jacek R.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2007-12-01
- Volume
- 36
- Issue
- 2
- Pages
- 570-577
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC2241850
- OpenAlex
- W2044731117
- Cited by
- 163
- References
- 35
- Citations by year
- 2026: 6 · 2025: 5 · 2024: 6 · 2023: 5 · 2022: 8 · 2021: 9 · 2020: 14 · 2019: 9 · 2018: 8 · 2017: 13 · 2016: 13 · 2015: 13 · 2014: 14 · 2013: 12 · 2012: 7
- FWCI
- 1.99
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc
- Locations
- Nucleic Acids Research (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- European Commission
- Uniwersytet Medyczny im. Piastów Slaskich we Wroclawiu
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- post-translational modification, histones, core histones, linker histones, high mobility group proteins, chromatin regulation, epigenetic regulation, nucleosome, DNA binding, nuclear proteins
- MeSH terms
- Aldehydes, Animals, Chromatin, Chromosomal Proteins, Non-Histone, High Mobility Group Proteins, Histones, Humans, Lysine, Mice, Inbred C57BL, Nuclear Proteins, Protein Processing, Post-Translational, Cell Line, Tumor, Mice, Tandem Mass Spectrometry
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