Secondary Structure Model of the Coat Protein Gene of Turnip Yellow Mosaic Virus RNA: Long, C-Rich, Single-Stranded Regions

• Published in: Virology (New York, N.Y.) N.Y.), 1996-10, Vol.224 (1), p.43-54
• Main Authors: Hellendoorn, Koen, Mat, Anton W., Gultyaev, Alexander P., Pleij, Cornelis W.A.
• Format: Article
• Language: English
• Subjects: Base Sequence; Capsid - genetics; Computer Simulation; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; RNA, Viral - chemistry; Tymovirus - genetics; Tymovirus - isolation & purification; VIRUS DE LAS PLANTAS; VIRUS DES VEGETAUX
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1006/viro.1996.0505

The RNA of all tymoviruses, a group of ssRNA plant viruses, has a base composition that is different from that of most other viruses. The excess of cytosines (35–42%) and the low number of guanosines (15–17%) must impel an RNA structure with a relatively low amount of base pairing and a high incidence of unpaired cytosines. These unpaired cytosines probably function in RNA–protein interactions. To gain insight into the way the RNA is positioned inside the virion, the secondary structure has been determined of a part of TYMV RNA, including the so-called tymobox, the coat protein gene, and the 3′ untranslated region, by structure probing, sequence comparison, and computer predictions. Conservation of secondary structure elements in tymoviruses is not high and does not parallel the conservation of the primary structure. A combination of structure prediction and probing experiments, however, results in a model consisting of structured domains of 100–200 nucleotides interspersed by long unpaired cytosine-rich regions. The latter may interact with the coat protein inside the virion. The structure of some functionally interesting regions of the 3′ part of TYMV RNA is also discussed.