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CROSSTALK OF VIRAL MOVEMENT PROTEIN AND PLASMODESMATA WITH PHOSPHORYLATION

Research Project

Project/Area Number 07660064
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeSingle-year Grants
Section一般
Research Field 植物保護
Research InstitutionTEIKYO UNIVERSITY

Principal Investigator

OKADA Yosimi (1996)  TEIKYO UNIVERSITY SCHOOL OF SCIENCE AND ENGINEERING PROFESSOR, 理工学部, 教授 (30011703)

池田 亮二 (1995)  帝京大学, 理工学部, 助手 (60222907)

Co-Investigator(Kenkyū-buntansha) 岡田 吉美  帝京大学, 理工学部, 教授 (30011703)
Project Period (FY) 1995 – 1996
Project Status Completed (Fiscal Year 1996)
Budget Amount *help
¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1996: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1995: ¥1,100,000 (Direct Cost: ¥1,100,000)
KeywordsTobacco Mosaic Virus / 30K Protein / Phosphorylation / Cell-to-Cell Movement / Viral Movement Protein / ウイルス移行蛋白質
Research Abstract

Tobamovirus movement proteins (MPs) facilitate virus spread through plasmodesmata by cellular and molecular mechanisms that are not yet fully understood. The MP of tomato mosaic tobamovirus (ToMV) is synthesized in early stages of infection and is phophorylated in vivo. We determined that serine 37 and serine 238 in ToMV MP are sites of phosphorylation through in vivo labeling, trypsin digestion, and analysis of natural and directed mutants of the MP.Substituting serine at position 37to Ala, Thr, Asp, and Glu in the MP of virus constructs produced viruses that are unable to cause symptoms on either local lesion or systemic tobacco or tomato hosts. By contrast, mutation of serine 238 to Ala did not affect the infectivity of the virus. Threonine at residue 37 can be phosphorylated in vivo as well as wild type MP.The data indicated a possibility that negative charge at position 37 in MP endowed viruses an ability to localize on microtubes.

Report

(3 results)
  • 1996 Annual Research Report   Final Research Report Summary
  • 1995 Annual Research Report

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Published: 1995-04-01   Modified: 2016-04-21  

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