Association of human mitochondrial lysyl-tRNA synthetase with HIV-1 GagPol does not require other viral proteins

Lydia Kobbi, José Dias, Martine Comisso, Marc Mirande
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引用次数: 3

Abstract

In human, the cytoplasmic (cLysRS) and mitochondrial (mLysRS) species of lysyl-tRNA synthetase are encoded by a single gene. Following HIV-1 infection, mLysRS is selectively taken up into viral particles along with the three tRNALys isoacceptors. The GagPol polyprotein precursor is involved in this process. With the aim to reconstitute in vitro the HIV-1 tRNA3Lys packaging complex, we first searched for the putative involvement of another viral protein in the selective viral hijacking of mLysRS only. After screening all the viral proteins, we observed that Vpr and Rev have the potential to interact with mLysRS, but that this association does not take place at the level of the assembly of mLysRS into the packaging complex. We also show that tRNA3Lys can form a ternary complex with the two purified proteins mLysRS and the Pol domain of GagPol, which mimicks its packaging complex.

Abstract Image

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人类线粒体赖氨酸- trna合成酶与HIV-1 GagPol的关联不需要其他病毒蛋白
在人类中,赖氨酸- trna合成酶的细胞质(cLysRS)和线粒体(mLysRS)是由一个基因编码的。在HIV-1感染后,mLysRS与三种tRNALys同工受体一起被选择性地吸收到病毒颗粒中。GagPol多蛋白前体参与了这一过程。为了在体外重建HIV-1 tRNA3Lys包装复合体,我们首先寻找另一种可能参与选择性病毒劫持mLysRS的病毒蛋白。在对所有病毒蛋白进行筛选后,我们观察到Vpr和Rev具有与mLysRS相互作用的潜力,但这种相互作用并不发生在mLysRS组装到包装复合物的水平上。我们还发现tRNA3Lys可以与两个纯化蛋白mLysRS和GagPol的Pol结构域形成三元配合物,这模仿了其包装复合物。
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