Hacking the sexual program of green algae by functional polyamides
| Project/Area Number |
18K19337
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| Research Category |
Grant-in-Aid for Challenging Research (Exploratory)
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| Allocation Type | Multi-year Fund |
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| Review Section |
Medium-sized Section 44:Biology at cellular to organismal levels, and related fields
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| Research Institution | Kyoto University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
杉山 弘 京都大学, 理学研究科, 教授 (50183843)
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| Project Period (FY) |
2018-06-29 – 2021-03-31
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| Project Status |
Completed (Fiscal Year 2020)
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| Budget Amount *help |
¥6,370,000 (Direct Cost: ¥4,900,000、Indirect Cost: ¥1,470,000)
Fiscal Year 2019: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2018: ¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
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| Keywords | 機能性ポリアミド / 緑藻クラミドモナス / 接合 / 細胞透過性 / 緑藻 / 生殖 / 生殖プログラム / シスエレメント |
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| Outline of Final Research Achievements |
Functional polyamide is an artificial chemical that binds directly to a specific target sequence. The target sequence can be arbitrarily designed and applied to suppress the expression of target genes. Using this technology, we analyzed ZYRE, a cis-element of the zygote specific genes of the unicellular green alga Chlamydomonas. The first barrier in this research was the improvement of cell permeability, which was solved by the addition of Arginine and TAMRA. RT-qPCR analysis confirmed the repression of zygote specific gene expression by polyamide treatment targeting ZYRE, supporting the importance of ZYRE in the zygote-specific gene expression in Chlamydomonas.
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| Academic Significance and Societal Importance of the Research Achievements |
機能性ポリアミドは狙った特定塩基配列に直接結合する人工化学物質であり、その標的配列は任意にデザインでき、目的遺伝子の発現抑制や活性化に応用できる。しかし細胞透過性の問題が、これまで一つの障壁であった。今回の研究から、ポリアミドにアルギニンを付加したり、TAMRAで修飾することにより、その細胞透過性を向上させて遺伝子発現の抑制効果を検証できるようになったことから、より多くの生物種への応用の糸口が得られた。また、今回の解析の方法論は、様々な生物種におけるcis-elementの遺伝子発現制御における機能解析に応用できると期待される。
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Report
(4 results)
Research Products
(51 results)
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[Journal Article] The pentatricopeptide repeat protein PGR3 is required for the translation of petL and ndhG by binding their 5'UTRs.2021
Author(s)
Higashi, H., Kato, Y., Fujita, T., Iwasaki, S., Nakamura, M., Nishimura, Y., Takenaka, M., Shikanai, T.
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Journal Title
Plant Cell Physiol
Volume: -
Related Report
Peer Reviewed / Open Access
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[Journal Article] HBD1 protein with a tandem repeat of two HMG box domains is a DNA clip to organize chloroplast nucleoids in Chlamydomonas reinhardtii.2021
Author(s)
Takusagawa, M., Kobayashi, Y., Fukao, Y., Hidaka, K., Endo, M., Sugiyama, H., Hamaji, T., Kato, Y., Miyakawa, I., Misumi, O., Shikanai, T., Nishimura, Y.
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Journal Title
Proc. Natl. Acad. Sci. USA
Volume: -
NAID
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Peer Reviewed / Open Access
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[Journal Article] Three genomes in the algal genus Volvox reveal the fate of a haploid sex-determining region after a transition to homothallism2021
Author(s)
Yamamoto, K., Hamaji, T., Kawai-Toyooka, H., Matsuzaki, R., Takahashi, F., Nishimura, Y., Kawachi, M., Noguchi, H., Minakuchi, Y., Umen, J.G., Toyoda, A., Nozaki, H.
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Journal Title
Proc. Natl. Acad. Sci. USA
Volume: -
Related Report
Peer Reviewed / Open Access
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[Journal Article] Isolation and characterization of Chlamydomonas autophagy-related mutants in nutrient-deficient conditions.2018
Author(s)
Kajikawa, M., Yamauchi, M., Shinkawa, H., Tanaka, M., Hatano, K., Nishimura, Y., Kato, M., Fukuzawa, H.
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Journal Title
Plant Cell Physiology
Volume: 60
Issue: 1
Pages: 126-138
DOI
Related Report
Peer Reviewed / Open Access
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[Presentation] Dynamic Network Structure of Chloroplast Nucleoids.2018
Author(s)
Yoshiki Nishimura, Yusuke Kobayashi, Yoshitaka Kamimura, Osami Misumi, Toshiharu Shikanai, Mari Takusagawa, Yusuke Kobayashi, Yoichiro Fukao, Isamu Miyakawa, Toshiharu Shikanai.
Organizer
18th International Conference on the Cell and Molecular Biology of Chlamydomonas
Related Report
Int'l Joint Research
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[Presentation] 第14回植物縦横無尽の会2018
Author(s)
Mari Takusagawa, Yusuke Kobayashi, Yoichiro Fukao, Isamu Miyakawa, Toshiharu Shikanai, Osami Misumi, and Yoshiki Nishimura
Organizer
Organelle nucleoid-associated HMG-box proteins may have been evolved independently through tandem domain duplications.
Related Report
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