Publication Type:Journal Article
Source:Virology, Volume 402, Number 1, p.177-86 (2010)
ISBN:1096-0341 (Electronic)<br/>0042-6822 (Linking)
Keywords:3' Untranslated Regions, Base Sequence, Luteovirus/ physiology, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Protein Biosynthesis, RNA, Messenger/chemistry/ genetics, RNA, Viral/chemistry/ genetics, Viral Proteins/ biosynthesis
The 3' untranslated regions (UTRs) of many plant viral RNAs contain cap-independent translation elements (3' CITEs). Among the 3' CITEs, the Barley yellow dwarf virus (BYDV)-like translation elements (BTEs) form a structurally variable and widely distributed group. Viruses in three genera were known to harbor 3' BTEs, defined by the presence of a 17-nt consensus sequence. To understand BTE function, knowledge of phylogenetically conserved structure is essential, yet the secondary structure has been determined only for the BYDV BTE. Here we show that Rose spring dwarf-associated luteovirus, and two viruses in a fourth genus, Umbravirus, contain functional BTEs, despite deviating in the 17nt consensus sequence. Structure probing by selective 2'-hydroxyl acylation and primer extension (SHAPE) revealed conserved and highly variable structures in BTEs in all four genera. We conclude that BTEs tolerate striking evolutionary plasticity in structure, while retaining the ability to stimulate cap-independent translation.
Wang, Zhaohui<br/>Kraft, Jelena J<br/>Hui, Alice Y<br/>Miller, W Allen<br/>R01 GM067104/GM/NIGMS NIH HHS/United States<br/>R01 GM067104-06/GM/NIGMS NIH HHS/United States<br/>Research Support, N.I.H., Extramural<br/>Research Support, Non-U.S. Gov't<br/>United States<br/>Virology. 2010 Jun 20;402(1):177-86. doi: 10.1016/j.virol.2010.03.025. Epub 2010 Apr 13.