Tyrosine phosphorylation of the triple gene block protein 3 regulates cell-to-cell movement and protein interactions of Potato mop-top virus.
Functions of viral proteins can be regulated through phosphorylation by serine/threonine kinases in plants, but little is known about the involvement of tyrosine kinases in plant virus infection. In this study, TGBp3, one of the three movement proteins encoded by a triple gene block (TGB) of Potato mop-top virus (PMTV), was detected for the first time in PMTV-infected plants and found to be tyrosine phosphorylated. Phosphorylation sites (Tyr(87-89) and Tyr(120)) were located in two amino acid motifs conserved in the TGB-containing, rod-shaped plant viruses. Substitution of these tyrosine residues in both motifs was needed to abolish tyrosine phosphorylation of TGBp3. Substitution of Tyr(87-89) with alanine residues enhanced the interaction between TGBp3 and TGBp2 and inhibited cell-to-cell movement of PMTV. On the other hand, substitution of Tyr(120) with alanine resulted in no alteration in the interaction of TGBp3 with TGBp2, but the mutant virus was not infectious. The results suggest that tyrosine phosphorylation is a mechanism regulating the functions of plant virus movement proteins.
Department of Agricultural Sciences, University of Helsinki, Helsinki, Finland.
Olga
O
Samuilova
Johanna
J
Santala
Jari P T
JP
Valkonen
D020816:Amino Acid Motifs; D019943:Amino Acid Substitution; D054884:Host-Pathogen Interactions; D010766:Phosphorylation; D010940:Plant Proteins / Q000378:metabolism*; D053830:Plant Viral Movement Proteins / Q000378:metabolism*; D010942:Plant Viruses / Q000472:pathogenicity*; D025941:Protein Interaction Mapping; D011499:Protein Processing, Post-Translational; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D014026:Nicotiana
D010940:Plant Proteins; D053830:Plant Viral Movement Proteins; D011505:Protein-Tyrosine Kinases