Gene analysis of proteases from Lentinula edodes and Hypsizygus marmoreus
| Project/Area Number |
26870730
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Wood science
Forest science
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| Research Institution | Kinki University |
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Principal Investigator |
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| Project Period (FY) |
2014-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2015: ¥650,000 (Direct Cost: ¥500,000、Indirect Cost: ¥150,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | プロテアーゼ / シイタケ / ブナシメジ / きのこ / 子実体形成 / Lentinula edodes / Hypsizygus marmoreus |
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| Outline of Final Research Achievements |
Fruit-body formation of Basidiomycetes was accelerated by the addition of carboxyl protease inhibitor (S-PI), and no occurrence of fruit-body by the addition of metallo protease inhibitors (Talopeptin, Phosphramidon, and EDTA).Several putative protease genes were selected using ForestGEN (L. edodes whole genome database). Among them, g876 (putative Eukaryotic aspartyl protease) showed high expression in mycelium stage of the fungus. In fruit-body (primordium)stage, g10056 (Eukaryotic aspartyl protease), g584, g1220 (Peptidase family 28) and g4055 (Peptidase family M13) were expressed higher than other putative protease genes. It seemed that g10056, g584, g1220 and g4055 have important role on fruit-body formation in L. edodes.
On the other hand, phosphoramidon sensitive metalloprotease from Hypsizygus marmoreus was purified, and the gene was cloned. The protease gene sequence showed high similarity with Fungalysin (Peptidase M36 family).
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Report
(3 results)
Research Products
(7 results)
