Protein-RNA linkage and post-translational modifications of two sobemovirus VPgs.
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.
Department of Gene Technology, Tallinn University of Technology, Akadeemia tee 15, 12618 Tallinn, Estonia.
Allan
A
Olspert
Lauri
L
Peil
Eugénie
E
Hébrard
Denis
D
Fargette
Erkki
E
Truve
D000595:Amino Acid Sequence; D018554:Avena / Q000821:virology; D019143:Evolution, Molecular; D015967:Gene Expression Regulation, Viral / Q000502:physiology; D014644:Genetic Variation; D058977:Molecular Sequence Annotation; D012275:Oryza / Q000821:virology; D010935:Plant Diseases / Q000821:virology; D018515:Plant Leaves / Q000821:virology; D010942:Plant Viruses / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D012367:RNA, Viral / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D012367:RNA, Viral; D014764:Viral Proteins