Characterization of a Chlamydomonas low-TAG accumulation mutant tar1-1 in nitrogen-deficient conditions
| Project/Area Number |
25850068
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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 |
Applied biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 環境応答 / 栄養欠乏応答 / 植物生理学 / 光合成 / 脂質代謝 / トリアシルグリセロール / 代謝工学 / 藻類バイオテクノロジー / 植物分子生物学 / 藻類分子育種 |
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| Outline of Final Research Achievements |
Although microalgae accumulate triacylglycerol (TAG) in response to N-deficient (-N) conditions, the regulatory mechanisms are poorly understood. I identified a kinase, TAG accumulation regulator 1 (TAR1), which is a member of dual-specificity tyrosine-phosphorylation-regulated kinase family in a green alga, Chlamydomonas reinhardtii. Kinase domain of TAR1 demonstrated auto- and trans-phosphorylation activities. A tar1-1 mutant accumulated TAG to levels 0.1-fold of those of a wild-type strain in -N conditions. In -N conditions, tar1-1 maintained chlorophyll and photosynthetic activity. In -N conditions, global changes in expression levels of -N responsive genes in N assimilation and tetrapyrrole metabolism were noted between tar1-1 and wild-type cells. These results indicated that TAR1 is a regulator of TAG accumulation in -N conditions, and it functions in cell growth and repression of photosynthesis in -N conditions.
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Report
(3 results)
Research Products
(20 results)
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[Journal Article] Arachidonic acid-dependent carbon-eight volatile synthesis from wounded liverwort (Marchantia polymorpha)2015
Author(s)
Kihara, H., Tanaka, M., Yamato, K.T., Horibara, A., Yamada, A., Kita, S., Ishizaki, K., Kajikawa, M., Fukuzawa, H., Kohchi, T., Akakabe, Y. and Matsui, K.
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Journal Title
Phytochemistry
Volume: 107
Pages: 42-49
DOI
Related Report
Peer Reviewed / Open Access
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