Analyses of the roles of disulfide bond formation between the replication proteins of tomato mosaic virus in viral RNA replication
Project/Area Number |
24380029
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Partial Multi-year Fund |
Section | 一般 |
Research Field |
Plant pathology
|
Research Institution | National Institute of Agrobiological Sciences |
Principal Investigator |
ISHIKAWA Masayuki 独立行政法人農業生物資源研究所, 植物・微生物間相互作用研究ユニット, ユニット長 (70192482)
|
Co-Investigator(Renkei-kenkyūsha) |
ISHIBASHI Kazuhiro 独立行政法人農業生物資源研究所, 植物・微生物間相互作用研究ユニット, 任期付研究員 (20611742)
|
Research Collaborator |
CHUJO Tetsuya
|
Project Period (FY) |
2012-04-01 – 2015-03-31
|
Project Status |
Completed (Fiscal Year 2014)
|
Budget Amount *help |
¥18,850,000 (Direct Cost: ¥14,500,000、Indirect Cost: ¥4,350,000)
Fiscal Year 2014: ¥6,890,000 (Direct Cost: ¥5,300,000、Indirect Cost: ¥1,590,000)
Fiscal Year 2013: ¥7,020,000 (Direct Cost: ¥5,400,000、Indirect Cost: ¥1,620,000)
Fiscal Year 2012: ¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
|
Keywords | ウイルス / RNA / 複製 / タンパク質 / 植物 |
Outline of Final Research Achievements |
The 130K replication protein of a tobamovirus bound to a 5'-terminal ca. 70-nucleotide region of its genomic RNA to form a ribonucleoprotein complex named PMTC. The binding inhibited translation of the RNA and lead it to a replication pathway. The PMTC contained multiple molecules of the replication protein. Interestingly, free (non-membrane-bound) 130K protein did not bind tobamovirus RNA, but the Met-IR fragment that corresponded to the N-terminal two-thirds of the 130K protein did. Thus, 130K protein molecules likely recognize tobamovirus RNA before the completion of their synthesis.
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Report
(4 results)
Research Products
(17 results)