首页> 美国卫生研究院文献>The Journal of Biophysical and Biochemical Cytology >Actin Bound to the Heterogeneous Nuclear Ribonucleoprotein Hrp36 Is Associated with Balbiani Ring mRNA from the Gene to Polysomes
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Actin Bound to the Heterogeneous Nuclear Ribonucleoprotein Hrp36 Is Associated with Balbiani Ring mRNA from the Gene to Polysomes

机译:肌动蛋白绑定到异质核核糖核蛋白Hrp36是与从基因到多核糖体的Balbiani环mRNA相关联。

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摘要

In the salivary glands of the dipteran Chironomus tentans, a specific messenger ribonucleoprotein (mRNP) particle, the Balbiani ring (BR) granule, can be visualized during its assembly on the gene and during its nucleocytoplasmic transport. We now show with immunoelectron microscopy that actin becomes associated with the BR particle concomitantly with transcription and is present in the particle in the nucleoplasm. DNase I affinity chromatography experiments with extracts from tissue culture cells indicate that both nuclear and cytoplasmic actin are bound to the heterogeneous RNP (hnRNP) protein hrp36, but not to the hnRNP proteins hrp23 and hrp45. The interaction is likely to be direct as purified actin binds to recombinant hrp36 in vitro. Furthermore, it is demonstrated by cross linking that nuclear as well as cytoplasmic actin are bound to hrp36 in vivo. It is known that hrp36 is added cotranscriptionally along the BR mRNA molecule and accompanies the RNA through the nuclear pores and into polysomes. We conclude that actin is likely to be bound to the BR transcript via hrp36 during the transfer of the mRNA from the gene all the way into polysomes.
机译:在二倍体Chironomus tentans的唾液腺中,特定的信使核糖核蛋白(mRNP)颗粒,Balbiani环(BR)颗粒,可以在其组装到基因上以及在其核质运输过程中看到。现在,我们用免疫电子显微镜显示肌动蛋白与转录相关的BR颗粒相关联,并存在于核质中。使用组织培养细胞提取物进行的DNase I亲和层析实验表明,核和细胞质肌动蛋白均与异质RNP(hnRNP)蛋白hrp36结合,但不与hnRNP蛋白hrp23和hrp45结合。由于纯化的肌动蛋白在体外与重组hrp36结合,因此相互作用可能是直接的。此外,通过交联证明,核以及细胞质肌动蛋白在体内与hrp36结合。众所周知,hrp36沿着BR mRNA分子共转录添加,并伴随RNA通过核孔进入多核小体。我们得出结论,在将mRNA从基因转移到多核小体的过程中,肌动蛋白很可能通过hrp36与BR转录物结合。

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