Ribosomal protein L1 recognizes the same specific structural motif in its target sites on the autoregulatory mRNA and 23S rRNA.

Ribosomal protein L1 recognizes the same specific structural motif in its target sites on the autoregulatory mRNA and 23S rRNA.
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DOI:
10.1093/nar/gki194
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发表时间:
2005
影响因子:
14.9
通讯作者:
Piendl W
Piendl W
中科院分区:
生物学2区
文献类型:
--
作者:
Nevskaya N;Tishchenko S;Gabdoulkhakov A;Nikonova E;Nikonov O;Nikulin A;Platonova O;Garber M;Nikonov S;Piendl W

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核糖体蛋白 L1 的 RNA 结合能力引起了人们的极大兴趣,因为该蛋白具有作为核糖体蛋白结合 rRNA 和作为结合其 mRNA 的翻译阻遏蛋白的双重功能。在这里,我们报告了核糖体蛋白L1与其mRNA特定片段复合物的晶体结构,并将其与之前确定的L1与23S rRNA特定片段复合物的结构进行比较。在这两种复合物中,高度保守的 RNA 结构基序通过溶剂无法接近的 RNA-蛋白质氢键保守网络参与 L1 结合。这些相互作用应该负责蛋白质和 RNA 之间的特异性识别。大量额外的非保守 RNA-蛋白质氢键可稳定这两种复合物。这些非保守氢键的额外贡献使得核糖体复合物比监管复合物稳定得多。
The RNA-binding ability of ribosomal protein L1 is of profound interest since the protein has a dual function as a ribosomal protein binding rRNA and as a translational repressor binding its mRNA. Here, we report the crystal structure of ribosomal protein L1 in complex with a specific fragment of its mRNA and compare it with the structure of L1 in complex with a specific fragment of 23S rRNA determined earlier. In both complexes, a strongly conserved RNA structural motif is involved in L1 binding through a conserved network of RNA–protein H-bonds inaccessible to the solvent. These interactions should be responsible for specific recognition between the protein and RNA. A large number of additional non-conserved RNA–protein H-bonds stabilizes both complexes. The added contribution of these non-conserved H-bonds makes the ribosomal complex much more stable than the regulatory one.
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发表时间: 1998-09-01
期刊: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
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