Truncated yet functional viral protein produced via RNA polymerase slippage implies underestimated coding capacity of RNA viruses
| Autor: | Junya Abe, Ichiro Uyeda, Satoshi Naito, Yuka Hagiwara-Komoda, Go Atsumi, Masanao Sato, Atsushi J. Nagano, Keisuke Komoda, Mie N. Honjo, Sun Hee Choi, Junya Fukuda, Kenji S. Nakahara |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Viral protein viruses Potyvirus Reading frame RNA-dependent RNA polymerase Biology medicine.disease_cause Article Open Reading Frames Viral Proteins 03 medical and health sciences chemistry.chemical_compound Cistron RNA polymerase Tobacco medicine Gene Plant Diseases Genetics Multidisciplinary RNA DNA-Directed RNA Polymerases RNA-Dependent RNA Polymerase Open reading frame 030104 developmental biology chemistry |
| Zdroj: | Scientific Reports |
| ISSN: | 2045-2322 |
| Popis: | RNA viruses use various strategies to condense their genetic information into small genomes. Potyviruses not only use the polyprotein strategy, but also embed an open reading frame, pipo, in the P3 cistron in the –1 reading frame. PIPO is expressed as a fusion protein with the N-terminal half of P3 (P3N-PIPO) via transcriptional slippage of viral RNA-dependent RNA polymerase (RdRp). We herein show that clover yellow vein virus (ClYVV) produces a previously unidentified factor, P3N-ALT, in the +1 reading frame via transcriptional slippage at a conserved G1–2A6–7 motif, as is the case for P3N-PIPO. The translation of P3N-ALT terminates soon, and it is considered to be a C-terminal truncated form of P3. In planta experiments indicate that P3N-ALT functions in cell-to-cell movement along with P3N-PIPO. Hence, all three reading frames are used to produce functional proteins. Deep sequencing of ClYVV RNA from infected plants endorses the slippage by viral RdRp. Our findings unveil a virus strategy that optimizes the coding capacity. |
| Databáze: | OpenAIRE |
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