Structural anatomy of telomere OB proteins.
Structural anatomy of telomere OB proteins.
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DOI：
10.3109/10409238.2011.609295
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发表时间：
2011-10
影响因子：
6.5
通讯作者：
Horvath MP
中科院分区：
文献类型：
--
作者：
Horvath MP
端粒DNA结合蛋白在真核生物中保护染色体末端。这些蛋白质的一个亚组由一个或多个OB折叠构建，并与在末端发现的富含G+ T的单链DNA结合。所产生的DNA-OB蛋白复合物与其他端粒组分相互作用，以协调DNA保护和DNA合成的关键端粒功能。虽然第一个晶体和NMR结构很容易解释端粒末端的保护，但单链DNA如何成为合成新端粒DNA的引物和模板的图片只是最近才成为焦点。端粒OB折叠蛋白的新结构以及来自遗传和生化实验的见解对理解蛋白结合OB蛋白如何与DNA结合OB蛋白合作以招募端粒酶和DNA聚合酶用于端粒稳态做出了重大贡献。本文综述了端粒OB蛋白的结构以及来自复制蛋白A（RPA）组分的高度可比的结构，目的是为了解端粒OB蛋白的进化和保护端粒DNA合成的作用机制提供分子背景。
Telomere DNA-binding proteins protect the ends of chromosomes in eukaryotes. A subset of these proteins are constructed with one or more OB folds and bind with G+T-rich single-stranded DNA found at the extreme termini. The resulting DNA-OB protein complex interacts with other telomere components to coordinate critical telomere functions of DNA protection and DNA synthesis. While the first crystal and NMR structures readily explained protection of telomere ends, the picture of how single-stranded DNA becomes available to serve as primer and template for synthesis of new telomere DNA is only recently coming into focus. New structures of telomere OB fold proteins alongside insights from genetic and biochemical experiments have made significant contributions towards understanding how protein-binding OB proteins collaborate with DNA-binding OB proteins to recruit telomerase and DNA polymerase for telomere homeostasis. This review surveys telomere OB protein structures alongside highly comparable structures derived from replication protein A (RPA) components, with the goal of providing a molecular context for understanding telomere OB protein evolution and mechanism of action in protection and synthesis of telomere DNA.