Structure of the RNA-binding domain of telomerase: Implications for RNA recognition and binding
Structure of the RNA-binding domain of telomerase: Implications for RNA recognition and binding
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DOI：
10.1016/j.str.2007.09.007
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发表时间：
2007-11-01
期刊：
影响因子：
5.7
通讯作者：
Skordalakes, Emmanuel
中科院分区：
文献类型：
--
作者：
Rouda, Susan;Skordalakes, Emmanuel
端粒酶是一种核糖核蛋白复合物，它复制真核生物染色体的线性末端，从而解决了“复制结束问题”。TERT含有一个基本的普遍保守结构域（TRBD），它与全酶的RNA （TER）成分广泛接触，这种相互作用被认为促进了TERT/TER的组装和重复添加性。在这里，我们展示了嗜热四膜虫TRBD的高分辨率结构。几乎全螺旋结构包括适合TER结合的核酸结合折叠。由两个保守基序（CP基序和T基序）在蛋白表面形成的延伸袋构成TRBD的rna结合袋。这个口袋的宽度和化学性质表明它结合单链和双链RNA，可能是茎1和模板边界元件（TBE）。此外，该结构为该结构域在TERT/TER稳定和端粒酶重复添加过程中的作用提供了线索。
Telomerase, a ribonucleoprotein complex, replicates the linear ends of eukaryotic chromosomes, thus taking care of the "end of replication problem." TERT contains an essential and universally conserved domain (TRBD) that makes extensive contacts with the RNA (TER) component of the holoenzyme, and this interaction is thought to facilitate TERT/TER assembly and repeat-addition processivity. Here, we present a high-resolution structure of TRBD from Tetrahymena thermophila. The nearly all-helical structure comprises a nucleic acid-binding fold suitable for TER binding. An extended pocket on the surface of the protein, formed by two conserved motifs (CP and T motifs) comprises TRBD's RNA-binding pocket. The width and the chemical nature of this pocket suggest that it binds both single- and double-stranded RNA, possibly stem 1, and the template boundary element (TBE). Moreover, the structure provides clues into the role of this domain in TERT/TER stabilization and telomerase repeat-addition processivity.