Structural basis for transcriptional start site control of HIV-1 RNA fate
| Autor: | Aishwarya S. Iyer, Issac Chaudry, Seung H. Choi, Matthew R. Orellana, Tatiana Rodriguez, Bryce Edwards, Hannah Carter, Michael W. Lopresti, Siarhei Kharytonchyk, Karndeep Singh, Lindsay Glang, Kailan Stewart, Jana Hijji, Ubiomo Oboh, Alice Telesnitsky, Joshua D. Brown, David A. Case, Frances Grace Ghinger, Yash Desai, Dillion Francis, Michael F. Summers, Ghazal Becker, Patrick Chen |
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| Rok vydání: | 2020 |
| Předmět: |
Gene Expression Regulation
Viral RNA Caps Base pair Guanosine Article chemistry.chemical_compound Protein biosynthesis Humans splice RNA Messenger Base Pairing Nuclear Magnetic Resonance Biomolecular Regulation of gene expression Base Composition Multidisciplinary Chemistry EIF4E RNA Cell biology Eukaryotic Initiation Factor-4E Protein Biosynthesis HIV-1 RNA Viral Transcription Initiation Site 5' Untranslated Regions Function (biology) |
| Zdroj: | Science |
| ISSN: | 1095-9203 0036-8075 |
| Popis: | One guanosine determines transcript fate Transcripts of the HIV-1 RNA genome can be either spliced and translated into viral proteins or packaged into new virions as a progeny genome. The path taken depends on whether the transcript contains one guanosine at the 5′ terminus (1G) rather than two or three (2G or 3G). Brown et al. used nuclear magnetic resonance spectroscopy to show that 1G transcripts adopt a dimeric structure that sequesters a terminal cap required for translation and splicing but exposes sites that bind to the HIV-1 Gag protein, which recruits the genome during viral assembly. Conversely, 2G or 3G transcripts have the cap accessible, but Gag-binding sites are sequestered. Therefore, a single guanosine acts as a conformational switch to determine the fate of HIV-1 transcripts. Science , this issue p. 413 |
| Databáze: | OpenAIRE |
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