The connection domain in reverse transcriptase facilitates the in vivo annealing of tRNALys3 to HIV-1 genomic RNA.
The connection domain in reverse transcriptase facilitates the in vivo annealing of tRNALys3 to HIV-1 genomic RNA.
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DOI：
10.1186/1742-4690-1-33
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发表时间：
2004-10-19
期刊：
影响因子：
3.3
通讯作者：
Kleiman L
中科院分区：
文献类型：
--
作者：
Cen S;Niu M;Kleiman L
HIV-1逆转录的引物tRNA，tRNALys3，在病毒组装过程中被选择性地包装到病毒中，并与病毒基因组RNA退火。参与将tRNALys包装成HIV-1的核糖核蛋白复合体由Gag、GagPol、tRNALys、赖氨酰-tRNA合成酶(LysRS)和病毒基因组RNA组成。GAG通过与LysRS(一种tRNALys结合蛋白)的相互作用来靶向tRNALys进行病毒包装，而GagPol(拇指结构域)中的逆转录酶(RT)序列则与tRNALys结合。TRNALys3对病毒RNA的进一步退火需要GAG中的核衣壳(NC)序列，而不是NC序列GagPol。在这份报告中，我们进一步表明，虽然GagPol中的RT连接结构域不是tRNALys3包装到病毒中所必需的，但它是tRNALys3退火到病毒RNA基因组所必需的。
The primer tRNA for reverse transcription in HIV-1, tRNALys3, is selectively packaged into the virus during its assembly, and annealed to the viral genomic RNA. The ribonucleoprotein complex that is involved in the packaging and annealing of tRNALys into HIV-1 consists of Gag, GagPol, tRNALys, lysyl-tRNA synthetase (LysRS), and viral genomic RNA. Gag targets tRNALys for viral packaging through Gag's interaction with LysRS, a tRNALys-binding protein, while reverse transcriptase (RT) sequences within GagPol (the thumb domain) bind to tRNALys. The further annealing of tRNALys3 to viral RNA requires nucleocapsid (NC) sequences in Gag, but not the NC sequences GagPol. In this report, we further show that while the RT connection domain in GagPol is not required for tRNALys3 packaging into the virus, it is required for tRNALys3 annealing to the viral RNA genome.