| Project/Area Number |
04680260
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
分子遺伝学・分子生理学
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| Research Institution | Teikyo University |
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Principal Investigator |
WATANABE Yuichiro Teikyo University, Faculty of Science and Engineering, Associate Professor, 理工学部, 助教授 (60183125)
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| Project Period (FY) |
1992 – 1993
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| Project Status |
Completed (Fiscal Year 1993)
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| Budget Amount *help |
¥1,800,000 (Direct Cost: ¥1,800,000)
Fiscal Year 1993: ¥600,000 (Direct Cost: ¥600,000)
Fiscal Year 1992: ¥1,200,000 (Direct Cost: ¥1,200,000)
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| Keywords | tobacco mosaic virus / plant viruses / phosphorylation / cell-to-cell movement / plasmodesmata / 30kD protein / host specificity |
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| Research Abstract |
I have analyzed the interactin of plant viruses and host cells in relation to plasmodesmata using tobacco mosaic virus as a model. All plant viruses go through plasmodesmata to move one cell to another cell. The 30kd protein functions in this cell-to-cell movement process. The protein is localized in plasmodesmata ; immunoelectron microscopic observation detected a structure formed just after being synthesized before going to plasmodesmata. I have detected phosphorylation of the protein in plant cells. Ser 238 (total 264 amino acid residues) is phosphorylated actually. Still another Ser located between residues 234 to 261 is phosphorylated. The 30kD protein derivatives which can be phosphorylated can form the cytoplasmic structure in vivo. Phosphorylation might be involved in the resistance-breaking ability or sensitivity in some cases. The mutant 22 which can overcome Tm-22 gene has two important amino acid changes compared with wild type 30kD protein. One of the two is Ser 238 which is phosphorylated at least in non-resistant tomatoes. I have started to perform detection of in vitro phosphorylation activity using the 30kD protein expressed in E.coli. It is suggested that plasmodesmata is involved in nutrient-traffic and exchange of signals inside plants ; thus the phosphorylation of the protein localized in this plasmodesmata would give us much information.
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