@article{mbs:/content/journal/jgv/10.1099/0022-1317-82-7-1785, author = "Carrier, Karma and Xiang, Yu and Sanfaçon, Hélène", title = "Genomic organization of RNA2 of Tomato ringspot virus: processing at a third cleavage site in the N-terminal region of the polyprotein in vitro", journal= "Journal of General Virology", year = "2001", volume = "82", number = "7", pages = "1785-1790", doi = "https://doi.org/10.1099/0022-1317-82-7-1785", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-82-7-1785", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", abstract = "The proteinase of Tomato ringspot virus (genus Nepovirus) is responsible for proteolytic cleavage of the RNA2-encoded polyprotein (P2) at two cleavage sites, allowing definition of the domains for the movement protein (MP) and coat protein. In this study, we have characterized a third cleavage site in the N-terminal region of P2 using an in vitro processing assay and partial cDNA clones. Results from site-directed mutagenesis of putative cleavage sites suggest that cleavage occurs at dipeptide Q301/G. Cleavage at this site is predicted to result in the release of two proteins from the N-terminal region of P2: a 34 kDa protein located at the N terminus of P2 (assuming translation initiation at the first AUG codon) and a 71 kDa protein located immediately upstream of the MP domain. In contrast, only one protein domain is present in the equivalent region of the P2 polyprotein of other characterized nepoviruses.", }