T 细胞内抗原-1 蛋白 C 端 RNA 识别基序的结构见解。
A structural insight into the C-terminal RNA recognition motifs of T-cell intracellular antigen-1 protein.
机构信息
Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla-CSIC, Sevilla, Spain.
出版信息
FEBS Lett. 2011 Oct 3;585(19):2958-64. doi: 10.1016/j.febslet.2011.07.037. Epub 2011 Aug 11.
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 α-helix (α(1)) which protects its single tryptophan from the solvent exposure, even in the two-domain RRM23 context. The α(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.
T 细胞内抗原-1（TIA-1）通过识别 RNA 中的富含尿嘧啶序列来调节选择性前体 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（RRMs）和一个富含谷氨酰胺的结构域。在这里，我们对其 C 端 RRM2 和 RRM3 结构域进行了表征。值得注意的是，RRM3 含有一个额外的新型 N 端α-螺旋（α(1)），即使在包含两个结构域的 RRM23 结构域中，该螺旋也能保护其单个色氨酸免受溶剂暴露。α(1)几乎不会影响 RRM3 的热稳定性。相反，RRM2 使 RRM3 不稳定，表明这两个模块一起旋转，这可能会影响 TIA-1 的 RNA 结合活性。
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