Interaction of Tomato mosaic virus movement protein with tobacco RIO kinase

Kuniaki Yoshioka, Yasuhiko Matsushita, Masahiro Kasahara, Ken Ichi Konagaya, Hiroshi Nyunoya*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)


Tomato mosaic virus (ToMV) has a regulatory gene encoding a movement protein (MP) that is involved in the cell-to-cell movement of viral RNA through plasmodesmata. To identify the host cell factors interacting with ToMV MP, we used a recombinant MP probe to isolate cDNA clones from a phage expression library of Nicotiana tabacum by a far-Western screening method. One of the cDNA clones encoded an MP-interacting protein, MIP-T7, homologous to the yeast novel protein kinase, Rio1p. We isolated a full-length cDNA by RT-PCR. The putative gene product was designated NtRIO, and shared 33 and 73% amino acid identity with yeast and Arabidopsis RIO kinases, respectively. In vitro analyses using recombinant proteins showed that NtRIO also interacted with a different MP derived from Cucumber mosaic virus. NtRIO had autophosphorylation activity and phosphorylated ToMV MP. Addition of recombinant tobacco casein kinase 2 resulted in a marked increase in the phosphorylation of NtRIO. The interaction between NtRIO and ToMV MP was inhibited by phosphorylation of NtRIO.

Original languageEnglish
Pages (from-to)223-229
Number of pages7
JournalMolecules and Cells
Issue number2
Publication statusPublished - 2004 Apr 30
Externally publishedYes


  • Casein kinase 2
  • Far-western
  • Movement protein
  • Nicotiana tabacum
  • Plant virus
  • Protein interaction
  • Protein phosphorylation
  • RIO
  • TMV
  • Tomato mosaic virus

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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