| Budget Amount *help |
¥17,420,000 (Direct Cost: ¥13,400,000、Indirect Cost: ¥4,020,000)
Fiscal Year 2020: ¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2019: ¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2018: ¥6,500,000 (Direct Cost: ¥5,000,000、Indirect Cost: ¥1,500,000)
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| Outline of Final Research Achievements |
We analyzed the function of lysophosphatidic acid acyltransferase (LPAAT), which is responsible for the generation of sn-2 acyl chain diversity in bacterial membrane phospholipids. We identified a novel LPAAT, YihG, in Escherichia coli, and clarified its substrate specificity and its relationship to flagellar formation. We succeeded in purification of LPAAT of Thermus thermophilus HB8 and clarified its various properties. Mutant strains of Shewanella livingstonensis Ac10 with inactivated LPAAT paralogs, PlsC4 and PlsC5, were generated, and the substrate specificities of these LPAATs and the involvement of PlsC4 in low temperature adaptation were demonstrated.
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