| Project/Area Number |
23580054
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Horticulture/Landscape architecture
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| Research Institution | Kinki University |
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Principal Investigator |
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2011: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 果実軟化 / 細胞壁 / トマト果実 / β-ガラクトシダーゼ / 細胞壁分解酵素 / 基質特異性 / 構造解析 |
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| Research Abstract |
In tomato fruit, beta-galactosidase 4 (TBG4) is an enzyme responsible for fruit softening through the degradation of beta-(1,4)-galactan in the pericarp cell wall. To gain structural insight into the substrate specificity, we determined the crystal structures of TBG4 and its complex with beta-D-galactose. TBG4 was composed of a catalytic TIM barrel domain followed by three beta-sandwich domains. This structure is similar to other beta-galactosidase belong to GH35 families.
In addition, we determined the enzymatic properties and substrate specificities of TBG1. TBG4 has substrate recognition to beta-(1,4)-linkage, however, TBG1 has beta-(1,3) and beta-(1,6)-likage substrate.
In these results, TBG's act on the tomato cell wall during fruits development and maturation, and seberal stage of tomato fruits cell walls construct/reconstruct to some components sugar as a substrate against TBG's.
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