Histone benzoylation serves as an epigenetic mark for DPF and YEATS family proteins
| العنوان: | Histone benzoylation serves as an epigenetic mark for DPF and YEATS family proteins |
|---|---|
| المؤلفون: | Ning Hao, Xiangle Ren, Xiaohuan Guo, Yuanyuan Li, Xiaobing Shi, Yang Zhou, Zhaoyu Xue, Haitao Li, Da-Liang Wang |
| المصدر: | Nucleic Acids Research |
| بيانات النشر: | Oxford University Press (OUP), 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | Epigenomics, Models, Molecular, Chromosomal Proteins, Non-Histone, Protein Conformation, AcademicSubjects/SCI00010, Acylation, Crystallography, X-Ray, Cell Line, Substrate Specificity, Histones, Mice, 03 medical and health sciences, 0302 clinical medicine, Transcription (biology), Sodium Benzoate, Genetics, Animals, Humans, Histone code, Amino Acid Sequence, Epigenetics, Histone Acetyltransferases, 030304 developmental biology, Regulation of gene expression, 0303 health sciences, biology, Lysine, Gene regulation, Chromatin and Epigenetics, Recombinant Proteins, Cell biology, Bromodomain, DNA-Binding Proteins, Histone Code, Mice, Inbred C57BL, Histone, Acetylation, Multigene Family, 030220 oncology & carcinogenesis, biology.protein, Hydrophobic and Hydrophilic Interactions, Protein Processing, Post-Translational, Protein Binding, Transcription Factors |
| الوصف: | Histone modifications and their functional readout serve as an important mechanism for gene regulation. Lysine benzoylation (Kbz) on histones is a recently identified acylation mark associated with active transcription. However, it remains to be explored whether putative readers exist to recognize this epigenetic mark. Here, our systematic binding studies demonstrated that the DPF and YEATS, but not the Bromodomain family members, are readers for histone Kbz. Co-crystal structural analyses revealed a ‘hydrophobic encapsulation’ and a ‘tip-sensor’ mechanism for Kbz readout by DPF and YEATS, respectively. Moreover, the DPF and YEATS family members display subtle yet unique features to create somewhat flexible engagements of different acylation marks. For instance, YEATS2 but not the other YEATS proteins exhibits best preference for Kbz than lysine acetylation and crotonylation due to its wider ‘tip-sensor’ pocket. The levels of histone benzoylation in cultured cells or in mice are upregulated upon sodium benzoate treatment, highlighting its dynamic regulation. In summary, our work identifies the first readers for histone Kbz and reveals the molecular basis underlying Kbz recognition, thus paving the way for further functional dissections of histone benzoylation. |
| تدمد: | 1362-4962 0305-1048 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::975d9dfadf5a162a754827819bad6995Test https://doi.org/10.1093/nar/gkaa1130Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....975d9dfadf5a162a754827819bad6995 |
| قاعدة البيانات: | OpenAIRE |
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