保护蛋白和端粒染色质的结构生物学：碎片和未完成的拼图。

IF 3.8 3区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Biochemical Society transactions Pub Date : 2024-08-28 DOI:10.1042/BST20230300

Hongmiao Hu, Helen Linwen Yan, Thi Hoang Duong Nguyen

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引用次数: 0

摘要

由六个亚单位组成的保护蛋白复合物与哺乳动物端粒结合，保护端粒不触发多种 DNA 损伤反应途径。保护蛋白失去这种保护功能会对细胞产生有害影响。在这篇综述中，我们首先讨论了保护蛋白的结构研究，详细介绍了每个亚基和亚基间相互作用在保护染色体末端方面的贡献。然后，我们研究了端粒染色质动力学对端粒保护蛋白功能的影响。这些研究提供了宝贵的见解，并强调了未来研究必须应对的挑战，以获得高分辨率的保护蛋白结构。

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Structural biology of shelterin and telomeric chromatin: the pieces and an unfinished puzzle.

The six-subunit shelterin complex binds to mammalian telomeres and protects them from triggering multiple DNA damage response pathways. The loss of this protective function by shelterin can have detrimental effects on cells. In this review, we first discuss structural studies of shelterin, detailing the contributions of each subunit and inter-subunit interactions in protecting chromosome ends. We then examine the influence of telomeric chromatin dynamics on the function of shelterin at telomeres. These studies provide valuable insights and underscore the challenges that future research must tackle to attain high-resolution structures of shelterin.

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来源期刊

Biochemical Society transactions 生物-生化与分子生物学

CiteScore

7.80

自引率

0.00%

发文量

351

审稿时长

3-6 weeks

期刊介绍： Biochemical Society Transactions is the reviews journal of the Biochemical Society. Publishing concise reviews written by experts in the field, providing a timely snapshot of the latest developments across all areas of the molecular and cellular biosciences. Elevating our authors’ ideas and expertise, each review includes a perspectives section where authors offer comment on the latest advances, a glimpse of future challenges and highlighting the importance of associated research areas in far broader contexts.