拟南芥组蛋白乙酰转移酶复合体协调细胞质组蛋白乙酰化和核染色质可及性。

IF 12.5 1区 综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES
Chan-Juan Wu, Xin Xu, Dan-Yang Yuan, Zhen-Zhen Liu, Lian-Mei Tan, Yin-Na Su, Lin Li, She Chen, Xin-Jian He
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引用次数: 0

摘要

保守型B组蛋白乙酰转移酶被认为在真核生物细胞质中对新合成的组蛋白进行乙酰化。然而,它们在细胞核内调节染色质方面的作用尚不清楚。我们的研究表明,拟南芥B型组蛋白乙酰转移酶HAG2与组蛋白伴侣蛋白MSI2、MSI3和NASP以及组蛋白H3和H4相互作用,在细胞质和细胞核中形成复合物。在这个复合体中,HAG2和MSI2/3构成了细胞质中组蛋白H4乙酰化所必需的组蛋白乙酰化模块。此外,该模块与NASP一起调节组蛋白乙酰化,染色质可及性和细胞核中的基因转录。该复合物增强了转录起始位点附近的染色质可及性,同时降低了转录终止位点附近的可及性。我们的研究结果揭示了拟南芥B型组蛋白乙酰转移酶在细胞核中的独特作用,揭示了植物细胞质组蛋白乙酰化与核染色质调节之间的协调。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Arabidopsis histone acetyltransferase complex coordinates cytoplasmic histone acetylation and nuclear chromatin accessibility

Arabidopsis histone acetyltransferase complex coordinates cytoplasmic histone acetylation and nuclear chromatin accessibility
Conserved type B histone acetyltransferases are recognized for their role in acetylating newly synthesized histones in the cytoplasm of eukaryotes. However, their involvement in regulating chromatin within the nucleus remains unclear. Our study shows that the Arabidopsis thaliana type B histone acetyltransferase HAG2 interacts with the histone chaperones MSI2, MSI3, and NASP, as well as the histones H3 and H4, forming a complex in both the cytoplasm and the nucleus. Within this complex, HAG2 and MSI2/3 constitute a histone acetylation module essential for acetylating histone H4 in the cytoplasm. Furthermore, this module works together with NASP to regulate histone acetylation, chromatin accessibility, and gene transcription in the nucleus. This complex enhances chromatin accessibility near transcription start sites while reducing accessibility near transcription termination sites. Our findings reveal a distinct role for the Arabidopsis type B histone acetyltransferase in the nucleus, shedding light on the coordination between cytoplasmic histone acetylation and nuclear chromatin regulation in plants.
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来源期刊
Science Advances
Science Advances 综合性期刊-综合性期刊
CiteScore
21.40
自引率
1.50%
发文量
1937
审稿时长
29 weeks
期刊介绍: Science Advances, an open-access journal by AAAS, publishes impactful research in diverse scientific areas. It aims for fair, fast, and expert peer review, providing freely accessible research to readers. Led by distinguished scientists, the journal supports AAAS's mission by extending Science magazine's capacity to identify and promote significant advances. Evolving digital publishing technologies play a crucial role in advancing AAAS's global mission for science communication and benefitting humankind.
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