Olspert A. auteur aut IRD Peil L. auteur aut IRD Hébrard Eugénie auteur aut IRD Fargette Denis auteur aut IRD Truve E. auteur aut IRD text journalArticle eng text/pdf reformatted digital access 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. specialized 076 92 Part 2 445-452 2011 0022-1317 https://www.documentation.ird.fr/hor/PAR00006594 10.1099/vir.0.026476-0 0022-1317 [F B010065013] https://www.documentation.ird.fr/hor/PAR00006594 https://horizon.documentation.ird.fr/exl-doc/pleins_textes/divers15-10/010065013.pdf IRD - Base Horizon / Pleins textes 2011-04-07 2017-08-23 PAR00006594 fre