A structural insight into the C-terminal RNA recognition motifs of T-cell intracellular antigen-1 protein
A structural insight into the C-terminal RNA recognition motifs of T-cell intracellular antigen-1 protein
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DOI：
10.1016/j.febslet.2011.07.037
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发表时间：
2011-10-03
期刊：
影响因子：
3.5
通讯作者：
Diaz-Moreno, Irene
中科院分区：
文献类型：
--
作者：
Aroca, Angeles;Diaz-Quintana, Antonio;Diaz-Moreno, Irene
T 细胞胞内抗原 1 (TIA-1) 通过识别富含尿苷的 RNA 序列来调节选择性前 mRNA 剪接和 mRNA 翻译，从而在细胞稳态中发挥多效性作用。 TIA-1 包含三个 RNA 识别基序 (RRM) 和一个富含谷氨酰胺的结构域。在这里，我们表征了其 C 端 RRM2 和 RRM3 域。值得注意的是，RRM3 包含一个额外的新型 N 端 α 螺旋 (α(1))，即使在双结构域 RRM23 环境中，它也能保护其单个色氨酸免受溶剂暴露。 α(1)几乎不影响RRM3的热稳定性。相反，RRM2 使 RRM3 不稳定，表明两个模块一起翻滚，这可能会影响 TIA-1 的 RNA 结合活性。 (C) 2011 年欧洲生化学会联合会。由 Elsevier B.V. 出版。保留所有权利。
T-cell intracellular antigen-1 (TIA-1) plays a pleiotropic role in cell homeostasis through the regulation of alternative pre-mRNA splicing and mRNA translation by recognising uridine-rich sequences of RNAs. TIA-1 contains three RNA recognition motifs (RRMs) and a glutamine-rich domain. Here, we characterise its C-terminal RRM2 and RRM3 domains. Notably, RRM3 contains an extra novel N-terminal alpha-helix (alpha(1)) which protects its single tryptophan from the solvent exposure, even in the two-domain RRM23 context. The alpha(1) hardly affects the thermal stability of RRM3. On the contrary, RRM2 destabilises RRM3, indicating that both modules are tumbling together, which may influence the RNA binding activity of TIA-1. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.