Histone chaperones include a wide variety of proteins which associate with histones and regulate chromatin structure. The classic H2A–H2B type of histone chaperones, and the chromatin remodeling complex components possessing H2A–H2B chaperone activity, show a broad range of structures and functions. Rapid progress in the structural and functional study of H2A–H2B chaperones extends our knowledge about the epigenetic regulation of chromatin. In this review, we summarize the most recent advances in the understanding of the structure and function of H2A–H2B chaperones that interact with either canonical or variant H2A–H2B dimers. We discuss the current knowledge of the H2A–H2B chaperones, which present no preference for canonical and variant H2A–H2B dimers, describing how they interact with H2A–H2B to fulfill their functions. We also review recent advances of H2A variant-specific chaperones, demarcating how they achieve specific recognition for histone variant H2A.Z and how these interactions regulate chromatin structure by nucleosome editing. We highlight the universal mechanism underlying H2A–H2B dimers recognition by a large variety of histone chaperones. These findings will shed insight into the biological impacts of histone chaperone, chromatin remodeling complex, and histone variants in chromatin regulation.

中文翻译：

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在染色质调节中对组蛋白H2A-H2B分子伴侣的机理和结构研究。

组蛋白伴侣包括与组蛋白缔合并调节染色质结构的多种蛋白质。经典的H2A–H2B类型的组蛋白伴侣，以及具有H2A–H2B伴侣活性的染色质重塑复合物，具有广泛的结构和功能。H2A–H2B分子伴侣的结构和功能研究的快速进展扩展了我们对染色质的表观遗传调控的知识。在这篇综述中，我们总结了对H2A–H2B分子伴侣的结构和功能的理解的最新进展，这些分子与规范的或变异的H2A–H2B二聚体相互作用。我们讨论了H2A–H2B分子伴侣的当前知识，这些知识对经典的H2A–H2B二聚体及其变体没有偏爱，描述了它们如何与H2A–H2B相互作用以实现其功能。我们还回顾了H2A变体特异性伴侣蛋白的最新进展，描述了它们如何实现对组蛋白变体H2A.Z的特异性识别，以及这些相互作用如何通过核小体编辑调节染色质结构。我们着重介绍了多种组蛋白分子伴侣识别H2A–H2B二聚体的普遍机制。这些发现将使人们深入了解组蛋白伴侣，染色质重塑复合物和组蛋白变异体在染色质调节中的生物学影响。