Furnes Clemens, Arnesen Thomas, Askjaer Peter, Kjems Jørgen, Szilvay Anne Marie
Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway.
Retrovirology. 2005 Jun 10;2:39. doi: 10.1186/1742-4690-2-39.
The HIV-1 Rev regulatory protein binds as an oligomeric complex to viral RNA mediating nuclear export of incompletely spliced and non-spliced viral mRNAs encoding the viral structural proteins. However, the biological significance of the obligatory complex formation of Rev upon the viral RNA is unclear.
The activity of various fusion proteins based on the negative oligomerization-defect Rev mutant M4 was tested using Rev dependent reporter constructs. An artificial M4 mutant dimer and an M4 mutant containing an extra basic domain from the HTLV-I Rex protein exhibited nearly full activity when compared to wild type Rev.
Rev dimerization appears to be required to expose free basic domains whilst the Rev oligomeric complex remains bound to viral RNA via other basic domains.
HIV-1 Rev调节蛋白以寡聚复合物的形式与病毒RNA结合，介导编码病毒结构蛋白的未完全剪接和未剪接的病毒mRNA的核输出。然而，Rev在病毒RNA上形成必需复合物的生物学意义尚不清楚。
使用依赖Rev的报告构建体测试了基于负性寡聚化缺陷Rev突变体M4的各种融合蛋白的活性。与野生型Rev相比，人工M4突变体二聚体和含有来自HTLV-I Rex蛋白的额外碱性结构域的M4突变体表现出几乎完全的活性。
Rev二聚化似乎是暴露游离碱性结构域所必需的，而Rev寡聚复合物则通过其他碱性结构域与病毒RNA保持结合。
