Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 53, Issue -, Pages 169-177Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2018.10.001
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Funding
- Ministry of Science and Technology of China [2016YFA0500700]
- National Natural Science Foundation of China [91753203, 31725014]
- Tsinghua University Initiative Scientific Research Program
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Histone post-translational modifications are crucial epigenetic mechanisms regulating a variety of biological events. Besides histone lysine acetylation, a repertoire of acylation types have been identified, including formylation, propionylation, butyrylation, crotonylation, 2-hydroxyisobutyrylation, beta-hydroxybutyrylation, succinylation, malonylation, glutarylation and benzoylation. From a structural perspective, here we summarize the writers and erasers of histone acylations and explain the molecular basis of these enzymes catalyzing non-acetyl histone acylations with a focus on histone crotonylation and beta-hydroxybutyrylation. Histone acylation readout, non-histone acylations and metabolic regulation are also discussed in this review.
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