Structural insights into the interaction of the nuclear exosome helicase Mtr4 with the preribosomal protein Nop53.
Structural insights into the interaction of the nuclear exosome helicase Mtr4 with the preribosomal protein Nop53.
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DOI：
10.1261/rna.062901.117
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发表时间：
2017-12
期刊：
影响因子：
--
通讯作者：
Conti E
中科院分区：
文献类型：
--
作者：
Falk S;Tants JN;Basquin J;Thoms M;Hurt E;Sattler M;Conti E
核外泌体和相关的RNA解旋酶Mtr4参与多种核糖核蛋白颗粒（RNP）的加工，包括大核糖体亚基（60S）的成熟。酿酒葡萄球菌Mtr4直接与Nop53相互作用，Nop53是一种核糖体生物发生因子，存在于含有5.8S rRNA前体的60年代晚期颗粒中。Mtr4-Nop53相互作用在5.8S rRNA的成熟过程中起着关键作用，为核外泌体和60s前RNP提供了物理联系。Mtr4和另一个核糖体生物发生因子Utp18之间的类似相互作用将外泌体引导到更早的核糖体前颗粒。Nop53和Utp18含有一个类似的mtr4结合基序，称为arch-interacting motif （AIM）。在这里，我们报道了与Nop53相互作用区域结合的S. cerevisiae Mtr4的3.2 Å分辨率晶体结构，揭示了解旋酶的KOW结构域如何通过疏水和静电相互作用网络识别Nop53的AIM序列。与aim相互作用的残基在Mtr4中是保守的，而不存在于相关的细胞质解旋酶Ski2中，这使得Mtr4在识别不同的aim蛋白时具有特异性和多功能性。利用核磁共振（NMR），我们发现Mtr4的KOW结构域可以同时结合含有aim的蛋白质和相邻表面的结构化RNA，这表明它是如何停靠在RNPs上的。因此，外泌体相关解旋酶的KOW结构域似乎是从核糖体蛋白的KOW结构域进化而来的，并在核外泌体中作为rnp结合模块发挥作用。
The nuclear exosome and the associated RNA helicase Mtr4 participate in the processing of several ribonucleoprotein particles (RNP), including the maturation of the large ribosomal subunit (60S). S. cerevisiae Mtr4 interacts directly with Nop53, a ribosomal biogenesis factor present in late pre-60S particles containing precursors of the 5.8S rRNA. The Mtr4–Nop53 interaction plays a pivotal role in the maturation of the 5.8S rRNA, providing a physical link between the nuclear exosome and the pre-60S RNP. An analogous interaction between Mtr4 and another ribosome biogenesis factor, Utp18, directs the exosome to an earlier preribosomal particle. Nop53 and Utp18 contain a similar Mtr4-binding motif known as the arch-interacting motif (AIM). Here, we report the 3.2 Å resolution crystal structure of S. cerevisiae Mtr4 bound to the interacting region of Nop53, revealing how the KOW domain of the helicase recognizes the AIM sequence of Nop53 with a network of hydrophobic and electrostatic interactions. The AIM-interacting residues are conserved in Mtr4 and are not present in the related cytoplasmic helicase Ski2, rationalizing the specificity and versatility of Mtr4 in the recognition of different AIM-containing proteins. Using nuclear magnetic resonance (NMR), we show that the KOW domain of Mtr4 can simultaneously bind an AIM-containing protein and a structured RNA at adjacent surfaces, suggesting how it can dock onto RNPs. The KOW domains of exosome-associated helicases thus appear to have evolved from the KOW domains of ribosomal proteins and to function as RNP-binding modules in the context of the nuclear exosome.
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影响因子：
16
作者：
Kowalinski E;Kögel A;Ebert J;Reichelt P;Stegmann E;Habermann B;Conti E
通讯作者：
Conti E
影响因子：
7.3
作者：
Henras, Anthony K.;Plisson-Chastang, Celia;O'Donohue, Marie-Francoise;Chakraborty, Anirban;Gleizes, Pierre-Emmanuel
通讯作者：
Gleizes, Pierre-Emmanuel
影响因子：
14.9
作者：
Klauer AA;van Hoof A
通讯作者：
van Hoof A
影响因子：
64.5
作者：
Halbach, Felix;Reichelt, Peter;Conti, Elena
通讯作者：
Conti, Elena
DOI：
10.1007/978-1-4419-7841-7_8
发表时间：
2010-01-01
期刊：
RNA EXOSOME
影响因子：
--
作者：
Butler, J. Scott;Mitchell, Phil
通讯作者：
Mitchell, Phil