Dual recognition of H3K4me3 and H3K27me3 by a plant histone reader SHL
Autor: | Xinchen Lv, Ray N. Scheid, Jiamu Du, Rui Liu, Shuiming Qian, Xuehua Zhong, Melissa D. Boersma, Li Lu, Wei Chen, John M. Denu, Zhenlin Yang |
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Jazyk: | angličtina |
Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Science Arabidopsis General Physics and Astronomy macromolecular substances Biology Methylation General Biochemistry Genetics and Molecular Biology Article Histones 03 medical and health sciences Gene Expression Regulation Plant Histone code Epigenetics lcsh:Science Psychological repression Regulation of gene expression Homeodomain Proteins Multidisciplinary Models Genetic Arabidopsis Proteins food and beverages General Chemistry Chromatin Cell biology Histone Code 030104 developmental biology Histone biology.protein H3K4me3 Homeobox lcsh:Q |
Zdroj: | Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018) Nature Communications |
ISSN: | 2041-1723 |
Popis: | The ability of a cell to dynamically switch its chromatin between different functional states constitutes a key mechanism regulating gene expression. Histone mark “readers” display distinct binding specificity to different histone modifications and play critical roles in regulating chromatin states. Here, we show a plant-specific histone reader SHORT LIFE (SHL) capable of recognizing both H3K27me3 and H3K4me3 via its bromo-adjacent homology (BAH) and plant homeodomain (PHD) domains, respectively. Detailed biochemical and structural studies suggest a binding mechanism that is mutually exclusive for either H3K4me3 or H3K27me3. Furthermore, we show a genome-wide co-localization of SHL with H3K27me3 and H3K4me3, and that BAH-H3K27me3 and PHD-H3K4me3 interactions are important for SHL-mediated floral repression. Together, our study establishes BAH-PHD cassette as a dual histone methyl-lysine binding module that is distinct from others in recognizing both active and repressive histone marks. Histone mark reader proteins bind to particular histone modifications and regulate chromatin state. Here, Qian et al. show that the SHORT LIFE reader has a unique ability to recognize both activating and repressive histone marks and that these interactions enable SHORT LIFE to repress flowering in plants. |
Databáze: | OpenAIRE |
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