DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network.
DAXX adds a de novo H3.3K9me3 deposition pathway to the histone chaperone network.
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DOI：
10.1016/j.molcel.2023.02.009
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发表时间：
2023-04-06
期刊：
影响因子：
16
通讯作者：
Groth, Anja
中科院分区：
文献类型：
--
作者：
Carraro, Massimo;Hendriks, Ivo A.;Hammond, Colin M.;Solis-Mezarino, Victor;Volker-Albert, Moritz;Elsborg, Jonas D.;Weisser, Melanie B.;Spanos, Christos;Montoya, Guillermo;Rappsilber, Juri;Imhof, Axel;Nielsen, Michael L.;Groth, Anja
从组蛋白的生物合成到DNA沉积，需要大量的组蛋白伴侣来支持组蛋白。它们通过形成组蛋白辅助伴侣复合体进行合作，但核小体组装途径之间的串扰仍然是个谜。利用探索性相互作用学，我们定义了人组蛋白H3-H4伴侣之间在组蛋白伴侣网络中的相互作用。我们鉴定了以前未表征的组蛋白依赖复合体，并预测了ASF1和SPT2共伴侣复合体的结构，扩大了ASF1在组蛋白动力学中的作用。我们发现DAXX为组蛋白伴侣网络提供了一种独特的功能，在沉积到DNA之前，招募组蛋白甲基转移酶来促进新的组蛋白H3.3-H4上的H3K9me3催化。因此，DAXX为从头沉积H3K9me3和异染色质组装提供了分子机制。总而言之，我们的发现为理解细胞如何协调组蛋白供应并利用修饰的组蛋白的靶向沉积来支持特殊的染色质状态提供了一个框架。组蛋白H3-H4伴侣相互作用网络的全景表征组蛋白共伴侣复合体和组蛋白变体的特异性DAXX将新的H3.3-H4招募到与H3K9me3作者和读者的复合体中DAXX在向染色质Carraro等人供应新组蛋白的过程中刺激H3.3K9me3催化。绘制了组蛋白H3-H4伴侣网络，揭示了参与核小体组装的辅助伴侣关系，并揭示了组蛋白伴侣DAXX在沉积到DNA之前促进新的组蛋白H3.3的赖氨酸9三甲基化。DAXX的功能为异染色质的从头组装提供了分子机制。
A multitude of histone chaperones are required to support histones from their biosynthesis until DNA deposition. They cooperate through the formation of histone co-chaperone complexes, but the crosstalk between nucleosome assembly pathways remains enigmatic. Using exploratory interactomics, we define the interplay between human histone H3–H4 chaperones in the histone chaperone network. We identify previously uncharacterized histone-dependent complexes and predict the structure of the ASF1 and SPT2 co-chaperone complex, expanding the role of ASF1 in histone dynamics. We show that DAXX provides a unique functionality to the histone chaperone network, recruiting histone methyltransferases to promote H3K9me3 catalysis on new histone H3.3–H4 prior to deposition onto DNA. Hereby, DAXX provides a molecular mechanism for de novo H3K9me3 deposition and heterochromatin assembly. Collectively, our findings provide a framework for understanding how cells orchestrate histone supply and employ targeted deposition of modified histones to underpin specialized chromatin states. Panoramic view of the histone H3–H4 chaperone interaction network Characterization of histone co-chaperone complexes and histone variant specificities DAXX recruits new H3.3–H4 into complexes with H3K9me3 writers and readers DAXX stimulates H3.3K9me3 catalysis during the supply of new histones to chromatin Carraro et al. charted the histone H3–H4 chaperone network, revealing co-chaperone relationships involved in nucleosome assembly and unveiling that histone chaperone DAXX promotes lysine 9 tri-methylation of new histone H3.3 prior to deposition onto DNA. With its functionality, DAXX provides a molecular mechanism for de novo heterochromatin assembly.
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