Olspert A., Peil L., Hébrard Eugénie, Fargette Denis, Truve E. (2011). Protein-RNA linkage and post-translational modifications of two sobemovirus VPgs. Journal of General Virology, 92 (Part 2), p. 445-452. ISSN 0022-1317.
Titre du document
Protein-RNA linkage and post-translational modifications of two sobemovirus VPgs
Olspert A., Peil L., Hébrard Eugénie, Fargette Denis, Truve E.
Source
Journal of General Virology, 2011,
92 (Part 2), p. 445-452 ISSN 0022-1317
Sobemoviruses possess a viral genome-linked protein (VPg) attached to the 5' end of viral RNA. VPg is processed from the viral polyprotein. In the current study, Cocksfoot mottle virus (CfMV) and Rice yellow mottle virus (RYMV) VPgs were purified from virions and analysed by mass spectrometry. The cleavage sites in the polyprotein and thereof the termini of VPg were experimentally proven. The lengths of the mature VPgs were determined to be 78 and 79 aa residues, respectively. The amino acid residues covalently linked to RNA in the two VPgs were, surprisingly, not conserved; it is a tyrosine at position 5 of CfMV VPg and serine at position 1 of RYMV VPg. Phosphorylations were identified in CfMV and RYMV VPgs with two positionally similar locations T20/S14 and S71/S72, respectively. RYMV VPg contains an additional phosphorylation site at S41.
