RNA-RNA interaction is required for the formation of specific bicoid mRNA 3' UTR-STAUFEN ribonucleoprotein particles
RNA-RNA interaction is required for the formation of specific bicoid mRNA 3' UTR-STAUFEN ribonucleoprotein particles
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DOI：
10.1093/emboj/16.7.1751
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发表时间：
1997-04-01
期刊：
影响因子：
11.4
通讯作者：
NussleinVolhard, C
中科院分区：
文献类型：
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作者：
Ferrandon, D;Koch, I;NussleinVolhard, C
果蝇胚胎的前模式的形成取决于形态学双子（BCD）在卵形细胞前极的定位，staufen蛋白（st; iu）在定位的一个后期需要为了将BCD mRNA锚定在前细胞质中，我们先前证明了内源性STAU专门与注射BCD mRNA 3'-非翻译区域（UTR），导致形成沿有丝分裂纺锤体的微管INA指向方式的特征性RNA蛋白颗粒。 Stau在该体内测定中认识到的区域预计将形成涉及大型双链拉伸的三个茎环结构，在这里，我们表明stau相互作用需要在RNA定位信号中的茎的双链构象，即在另外，两个单链环之间的碱基对在粒子形成中起主要作用，这种环环相互作用是分子间的，而不是分子内；因此，RNA定位信号的二聚体或多聚体必须与这些颗粒中的stau相关，而BCD mRNA 3'UTR也可以在没有STAU的情况下在体外二聚体。因此，除了RNA-蛋白相互作用外，RNA-RNA相互作用可能与核糖核蛋白颗粒的形成一起进行运输和定位。
The formation of the anterior pattern of the Drosophila embryo is dependent on the localization of the mRNA of the morphogen Bicoid (bcd) to the anterior pole of the egg cell, Staufen protein (ST;IU) is required in a late step of the localization to anchor the bcd mRNA in the anterior cytoplasm, We have shown previously that endogenous STAU associates specifically with injected bcd mRNA 3'-untranslated region (UTR), resulting in the formation of characteristic RNA-protein particles that are transported along microtubules of the mitotic spindles ina directed manner. The regions recognized by STAU in this in vivo assay are predicted to form three stem-loop structures involving large double-stranded stretches, Here, we show that the STAU interaction requires a double-stranded conformation of the stems within the RNA localization signal, In addition, base pairing between two single-stranded loops plays a major role in particle formation, This loop-loop interaction is intermolecular, not intramolecular; thus dimers or multimers of the RNA localization signal must be associated with STAU in these particles, The bcd mRNA 3' UTR can also dimerize in vitro in the absence of STAU. Thus, in addition to RNA-protein interactions, RNA-RNA interaction might be involved in the formation of ribonucleoprotein particles for transport and localization.