Telomere capping proteins are structurally related to RPA with an additional telomere-specific domain
Telomere capping proteins are structurally related to RPA with an additional telomere-specific domain
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DOI：
10.1073/pnas.0909203106
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发表时间：
2009-11-17
影响因子：
11.1
通讯作者：
Wuttke, Deborah S.
中科院分区：
文献类型：
--
作者：
Gelinas, Amy D.;Paschini, Margherita;Wuttke, Deborah S.
端粒必须被封顶，以保持染色体的稳定性。保守的Stn1和Ten1蛋白是正确封顶端粒所必需的，尽管它们对端粒维持的作用机制细节尚不清楚。在这里，我们报道了酿酒酵母Stn1和裂殖酵母Ten1蛋白C-末端结构域的晶体结构。这些结构显示出与复制蛋白A复合体中相应亚基的惊人相似之处，进一步支持了端粒维持蛋白和DNA修复复合体之间的进化联系。我们的Stn1的结构和体内数据确定了一个新的结构域，该结构域已经进化为支持端粒在染色体维持中的特定作用。这些发现支持一种进化保守的DNA维持机制的模型，该机制是由于染色体结构复杂性的增加而发展起来的。
Telomeres must be capped to preserve chromosomal stability. The conserved Stn1 and Ten1 proteins are required for proper capping of the telomere, although the mechanistic details of how they contribute to telomere maintenance are unclear. Here, we report the crystal structures of the C-terminal domain of the Saccharomyces cerevisiae Stn1 and the Schizosaccharomyces pombe Ten1 proteins. These structures reveal striking similarities to corresponding subunits in the replication protein A complex, further supporting an evolutionary link between telomere maintenance proteins and DNA repair complexes. Our structural and in vivo data of Stn1 identify a new domain that has evolved to support a telomere-specific role in chromosome maintenance. These findings endorse a model of an evolutionarily conserved mechanism of DNA maintenance that has developed as a result of increased chromosomal structural complexity.