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Title: Truncated yet functional viral protein produced via RNA polymerase slippage implies underestimated coding capacity of RNA viruses
Authors: Hagiwara-Komoda, Yuka
Choi, Sun Hee
Sato, Masanao
Atsumi, Go
Abe, Junya
Fukuda, Junya
Honjo, Mie N.
Nagano, Atsushi J.
Komoda, Keisuke
Nakahara, Kenji S.
Uyeda, Ichiro
Naito, Satoshi
Author's alias: 本庄, 三恵
Issue Date: 22-Feb-2016
Publisher: Nature Publishing Group
Journal title: Scientific Reports
Volume: 6
Thesis number: 21411
Abstract: 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.
Rights: This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
URI: http://hdl.handle.net/2433/216021
DOI(Published Version): 10.1038/srep21411
PubMed ID: 26898356
Appears in Collections:Journal Articles

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