@article{fdi:010065013,
  title = {{P}rotein-{RNA} linkage and post-translational modifications of two sobemovirus {VP}gs},
  author = {{O}lspert, {A}. and {P}eil, {L}. and {H}{\'e}brard, {E}ug{\'e}nie and {F}argette, {D}enis and {T}ruve, {E}.},
  editor = {},
  language = {{ENG}},
  abstract = {{S}obemoviruses possess a viral genome-linked protein ({VP}g) attached to the 5' end of viral {RNA}. {VP}g is processed from the viral polyprotein. {I}n the current study, {C}ocksfoot mottle virus ({C}f{MV}) and {R}ice yellow mottle virus ({RYMV}) {VP}gs were purified from virions and analysed by mass spectrometry. {T}he cleavage sites in the polyprotein and thereof the termini of {VP}g were experimentally proven. {T}he lengths of the mature {VP}gs were determined to be 78 and 79 aa residues, respectively. {T}he amino acid residues covalently linked to {RNA} in the two {VP}gs were, surprisingly, not conserved; it is a tyrosine at position 5 of {C}f{MV} {VP}g and serine at position 1 of {RYMV} {VP}g. {P}hosphorylations were identified in {C}f{MV} and {RYMV} {VP}gs with two positionally similar locations {T}20/{S}14 and {S}71/{S}72, respectively. {RYMV} {VP}g contains an additional phosphorylation site at {S}41.},
  keywords = {},
  booktitle = {},
  journal = {{J}ournal of {G}eneral {V}irology},
  volume = {92},
  numero = {{P}art 2},
  pages = {445--452},
  ISSN = {0022-1317},
  year = {2011},
  DOI = {10.1099/vir.0.026476-0},
  URL = {https://www.documentation.ird.fr/hor/fdi:010065013},
}