Suppr超能文献

人类线粒体赖氨酰 - tRNA合成酶与HIV - 1 GagPol的结合不需要其他病毒蛋白。

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

作者信息

Kobbi Lydia, Dias José, Comisso Martine, Mirande Marc

机构信息

Institute for Integrative Biology of the Cell (I2BC), Université Paris-Saclay, CEA, CNRS, Université Paris-Sud, 1 avenue de la Terrasse, 91190 Gif-sur-Yvette, France.

出版信息

Biochim Open. 2016 Mar 5;2:52-61. doi: 10.1016/j.biopen.2016.02.004. eCollection 2016 Jun.

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 tRNA isoacceptors. The GagPol polyprotein precursor is involved in this process. With the aim to reconstitute in vitro the HIV-1 tRNA 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 tRNA can form a ternary complex with the two purified proteins mLysRS and the Pol domain of GagPol, which mimicks its packaging complex.

摘要

在人类中,赖氨酰 - tRNA合成酶的细胞质(cLysRS)和线粒体(mLysRS)种类由单个基因编码。HIV - 1感染后,mLysRS与三种同功tRNA一起被选择性地摄取到病毒颗粒中。GagPol多蛋白前体参与了这一过程。为了在体外重建HIV - 1 tRNA包装复合物,我们首先寻找另一种病毒蛋白在仅对mLysRS进行选择性病毒劫持中的假定作用。在筛选了所有病毒蛋白后,我们观察到Vpr和Rev有可能与mLysRS相互作用,但这种关联并非发生在mLysRS组装到包装复合物的水平。我们还表明,tRNA可以与两种纯化的蛋白mLysRS和GagPol的Pol结构域形成三元复合物,该复合物模拟了其包装复合物。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/9522/5889485/ca858c4b4bde/gr1.jpg

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验