Defective tobamovirus movement protein lacking wild-type phosphorylation sites can be complemented by substitutions found in revertants.

@article{Kawakami2003DefectiveTM,
  title={Defective tobamovirus movement protein lacking wild-type phosphorylation sites can be complemented by substitutions found in revertants.},
  author={Shigeki Kawakami and Koichi Hori and Daijiro Hosokawa and Yoshimi Okada and Yuichiro Watanabe},
  journal={Journal of virology},
  year={2003},
  volume={77 2},
  pages={1452-61}
}
We reported previously that the movement protein (MP) of tomato mosaic tobamovirus is phosphorylated, and we proposed that MP phosphorylation is important for viral pathogenesis. Experimental data indicated that phosphorylation enhances the stability of MP in vivo and enables the protein to assume the correct intracellular location to perform its function. A mutant virus designated 37A238A was constructed; this virus lacked two serine residues within the MP, which prevented its phosphorylation… CONTINUE READING

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