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The three-way junction structure of the HIV-1 PBS-segment binds host enzyme important for viral infectivity

Nucleic Acids Res. 2021-06; 
Zhenwei Song, Thomas Gremminger, Gatikrushna Singh, Yi Cheng, Jun Li, Liming Qiu, Juan Ji, Margaret J Lange, Xiaobing Zuo, Shi-Jie Chen, Xiaoqin Zou, Kathleen Boris-Lawrie, Xiao Heng
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GenParts™ DNA Fragments The PBS mutations in pNL4–3-CMV-EGFP for infectivity assays were generated by multiple DNA fragment assembly using primers listed in Supplementary Tables S1 and S2. (GenBuilder Cloning Kit, GenScript). Get A Quote

摘要

HIV-1 reverse transcription initiates at the primer binding site (PBS) in the viral genomic RNA (gRNA). Although the structure of the PBS-segment undergoes substantial rearrangement upon tRNALys3 annealing, the proper folding of the PBS-segment during gRNA packaging is important as it ensures loading of beneficial host factors. DHX9/RNA helicase A (RHA) is recruited to gRNA to enhance the processivity of reverse transcriptase. Because the molecular details of the interactions have yet to be defined, we solved the solution structure of the PBS-segment preferentially bound by RHA. Evidence is provided that PBS-segment adopts a previously undefined adenosine-rich three-way junction structure encompassing the prime... More

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