Chromatin attachment to the nuclear matrix represses hypocotyl elongation in Arabidopsis thaliana

The nuclear matrix is a nuclear compartment that has diverse functions in chromatin regulation and transcription. However, how this structure influences epigenetic modifications and gene expression in plants is largely unknown. In this study, we show that a nuclear matrix binding protein, AHL22, tog...

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Published in:Nature communications Vol. 15; no. 1; p. 1286
Main Authors: Xu, Linhao, Zheng, Shiwei, Witzel, Katja, Van De Slijke, Eveline, Baekelandt, Alexandra, Mylle, Evelien, Van Damme, Daniel, Cheng, Jinping, De Jaeger, Geert, Inzé, Dirk, Jiang, Hua
Format: Journal Article
Language:English
Published: London Nature Publishing Group UK 12-02-2024
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Summary:The nuclear matrix is a nuclear compartment that has diverse functions in chromatin regulation and transcription. However, how this structure influences epigenetic modifications and gene expression in plants is largely unknown. In this study, we show that a nuclear matrix binding protein, AHL22, together with the two transcriptional repressors FRS7 and FRS12, regulates hypocotyl elongation by suppressing the expression of a group of genes known as SMALL AUXIN UP RNAs ( SAURs ) in Arabidopsis thaliana . The transcriptional repression of SAURs depends on their attachment to the nuclear matrix. The AHL22 complex not only brings these SAURs, which contain matrix attachment regions (MARs), to the nuclear matrix, but it also recruits the histone deacetylase HDA15 to the SAUR loci. This leads to the removal of H3 acetylation at the SAUR loci and the suppression of hypocotyl elongation. Taken together, our results indicate that MAR-binding proteins act as a hub for chromatin and epigenetic regulators. Moreover, we present a mechanism by which nuclear matrix attachment to chromatin regulates histone modifications, transcription, and hypocotyl elongation. The role of the nuclear matrix in plant nuclei is unclear. Here the authors reveal that nuclear matrix-associated proteins act as a regulatory hub, recruiting both DNA and transcriptional repressors to the nuclear matrix
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ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-024-45577-5