Genetic interactions suggest multiple distinct roles of the arch and core helicase domains of Mtr4 in Rrp6 and exosome function.
Genetic interactions suggest multiple distinct roles of the arch and core helicase domains of Mtr4 in Rrp6 and exosome function.
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DOI：
10.1093/nar/gks1013
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发表时间：
2013-01-07
影响因子：
14.9
通讯作者：
van Hoof A
中科院分区：
文献类型：
--
作者：
Klauer AA;van Hoof A
RNA外泌体负责多种RNA加工和降解反应。RNA外泌体的活性和特异性被认为是由一些辅助因子控制的。Mtr4是一种必需的RNA依赖性腺苷三磷酸酶，是RNA外泌体所有核功能所必需的。Mtr4的晶体结构揭示了一个在RNA外泌体辅助因子Mtr4和Ski2中保守而在其他解旋酶中不存在的结构域，这表明它在外泌体激活中具有重要作用。Rrp6为核外泌体提供其三种核酸酶活性之一，先前的研究结果表明，arch结构域是Rrp6功能所特有的。在这里，我们报告了Mtr4和Rrp6的arch结构域之间的遗传相互作用不能用arch结构域单独作用于Rrp6依赖的加工反应来解释。具体来说，我们证明了拱形结构域不是所有Rrp6功能所必需的，并且拱形结构域也独立于Rrp6而起作用。最后，我们发现Mtr4的细胞质对应物Ski2的拱形结构域是Ski2功能所必需的，从而证实了这些辅助因子的拱形结构域独立于Rrp6发挥作用。
The RNA exosome is responsible for a wide variety of RNA processing and degradation reactions. The activity and specificity of the RNA exosome is thought to be controlled by a number of cofactors. Mtr4 is an essential RNA-dependent adenosine triphosphatase that is required for all of the nuclear functions of the RNA exosome. The crystal structure of Mtr4 uncovered a domain that is conserved in the RNA exosome cofactors Mtr4 and Ski2 but not in other helicases, suggesting it has an important role related to exosome activation. Rrp6 provides the nuclear exosome with one of its three nuclease activities, and previous findings suggested that the arch domain is specifically required for Rrp6 functions. Here, we report that the genetic interactions between the arch domain of Mtr4 and Rrp6 cannot be explained by the arch domain solely acting in Rrp6-dependent processing reactions. Specifically, we show that the arch domain is not required for all Rrp6 functions, and that the arch domain also functions independently of Rrp6. Finally, we show that the arch domain of Ski2, the cytoplasmic counterpart of Mtr4, is required for Ski2’s function, thereby confirming that the arch domains of these cofactors function independently of Rrp6.
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