Biochemical analysis of Hybrid type polyketide synthase Steely that produce multi-products
Project/Area Number |
15K01807
|
Research Category |
Grant-in-Aid for Scientific Research (C)
|
Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Biomolecular chemistry
|
Research Institution | Sophia University |
Principal Investigator |
SAITO Tamao 上智大学, 理工学部, 教授 (30281843)
|
Co-Investigator(Kenkyū-buntansha) |
森田 直樹 国立研究開発法人産業技術総合研究所, 生命工学領域, 研究グループ付 (60371085)
|
Project Period (FY) |
2015-04-01 – 2018-03-31
|
Project Status |
Completed (Fiscal Year 2017)
|
Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
Keywords | ポリケタイド / 生合成 / 微生物 |
Outline of Final Research Achievements |
Polyketide synthase “Steely” has a distinct structure that is a fusion of a type I and III polyketide synthases. One of them, SteelyB was identified to be responsible for the production of DIF-1 that induces (pre)stalk cells differentiation in the slug stage of D. discoideum development. We identified LCC-1, chlorinated benzofuran that accumulated in the stalk region of fruiting bodies as second product of SteelyB enzyme. NMR and Crystal structural analysis revealed the detailed structure of LCC-1. The result of chlorine labelling experiment showed that ChlA, a chlorinating enzyme that regulated DIF-1 production was also involved in biosynthetic pathway of LCC-1. The feeding experiment indicated that THPH, a DIF-1 polyketide backbone rescued the production of LCC-1 in stlB null mutant. From these results, we hypothesized that SteelyB and ChlA are also involved in the LCC-1 biosynthesis. These two enzymes change their localization and thus change the modifying enzymes to produce LCC-1
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Report
(4 results)
Research Products
(5 results)