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Identification of ‘erasers’ for lysine crotonylated histone marks using a chemical proteomics approach
Open accessAbstract
Posttranslational modifications (PTMs) play a crucial role in a wide range of biological processes. Lysine crotonylation (Kcr) is a newly discovered histone PTM that is enriched at active gene promoters and potential enhancers in mammalian cell genomes. However, the cellular enzymes that regulate the addition and removal of Kcr are unknown, which has hindered further investigation of its cellular functions. Here we used a chemical proteomics approach to comprehensively profile ‘eraser’ enzymes that recognize a lysine-4 crotonylated histone H3 (H3K4Cr) mark. We found that Sirt1, Sirt2, and Sirt3 can catalyze the hydrolysis of lysine crotonylated histone peptides and proteins. More importantly, Sirt3 functions as a decrotonylase to regulate histone Kcr dynamics and gene transcription in living cells. This discovery not only opens opportunities for examining the physiological significance of histone Kcr, but also helps to unravel the unknown cellular mechanisms controlled by Sirt3, that have previously been considered solely as a deacetylase.
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“Unsurprisingly, given the range of their potential substrates, sirtuins 1, 216 and 317 were shown to be decrotonylases in vitro.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [17]
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“To date, decrotonylase activity has been described for HDAC1-3 and Sirtuins 1-316–18,21,22.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [17]
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Metadata
- Authors
- Bao, X., Wang, Y., Li, X., Li, X.-M., Liu, Z., Yang, T., Wong, C. F., Zhang, J., Hao, Q., & Li, X. D.
- Affiliations
- University of Hong Kong (HK)
- Department of Chemistry, University of Hong Kong, Hong Kong, Hong Kong
- Corresponding author
- Hao, Quan
- Li, Xiang David
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2014-11-04
- Volume
- 3
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC4358366
- OpenAlex
- W2109845335
- Cited by
- 324
- References
- 45
- Citations by year
- 2026: 23 · 2025: 27 · 2024: 31 · 2023: 28 · 2022: 29 · 2021: 44 · 2020: 18 · 2019: 18 · 2018: 32 · 2017: 25 · 2016: 31 · 2015: 16 · 2014: 2
- FWCI
- 10.11
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- The HKU Scholars Hub (University of Hong Kong) (submittedVersion, cc-by-nc-nd)
- Funders
- Research Grants Council, University Grants Committee, Hong Kong (Early Career Scheme, HKU 709813P, General Research Fund, GRF766510, General Research Fund, GRF17303114)
- University of Hong Kong (Hung Hing Ying Physical Science Research Fund, 20373739)
- 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 › Histone Deacetylase Inhibitors Research
- Keywords
- lysine crotonylation, histone crotonylation, SIRT3, SIRT1, SIRT2, H3K4, histone modifications, transcriptional regulation, chemoproteomics
- MeSH terms
- Biotin, Crotonates, HeLa Cells, Histones, Humans, Hydrolysis, Isotope Labeling, Lysine, Models, Molecular, Peptides, Promoter Regions, Genetic, Protein Binding, Protein Processing, Post-Translational, Recombinant Proteins, Genome, Human, Streptavidin, Proteomics, Sirtuin 1, Sirtuin 2, Sirtuin 3, HEK293 Cells, Click Chemistry
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