Exploring the dynamism of chloroplastic chromosomes, nucleoids
Project/Area Number |
18H02460
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Research Category |
Grant-in-Aid for Scientific Research (B)
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Allocation Type | Single-year Grants |
Section | 一般 |
Review Section |
Basic Section 44030:Plant molecular biology and physiology-related
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Research Institution | Kyoto University |
Principal Investigator |
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Project Period (FY) |
2018-04-01 – 2021-03-31
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Project Status |
Completed (Fiscal Year 2021)
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Budget Amount *help |
¥17,290,000 (Direct Cost: ¥13,300,000、Indirect Cost: ¥3,990,000)
Fiscal Year 2020: ¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2019: ¥5,850,000 (Direct Cost: ¥4,500,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2018: ¥5,980,000 (Direct Cost: ¥4,600,000、Indirect Cost: ¥1,380,000)
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Keywords | 葉緑体DNA / 核様体 / 葉緑体核様体 / DNA ligase / DNA 修復 / 相同組換え / DNA リガーゼ / 葉緑体 / 葉緑体DNA複製・修復 / ゲノム安定性 |
Outline of Final Research Achievements |
Compaction of bulky DNA is a universal issue for all DNA-based life forms. Both Chloroplasts and mitochondria maintain their own multi-copy genomes organized as nucleoids, but the mechanism of DNA compaction remains obscure. Here, we discovered a chloroplast nucleoid protein (HBD1) that is highly similar to major mitochondrial nucleoid proteins transcription factor A, mitochondrial (TFAM), and ARS binding factor 2 protein (Abf2p) in terms of possessing two DNA-binding high mobility group box (HMG-box) domains. Our analyses of HBD1 based on DNA origami/atomic force microscopy showed that HBD1 is capable of compacting DNA by introducing U-turns and cross-strand bridges with the two HMG-box domains, indicating that proteins with two HMG-box domains could compact DNA in both mitochondrial and chloroplast nucleoids.
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Academic Significance and Societal Importance of the Research Achievements |
葉緑体において、2つのDNA結合部位(HMG-boxドメイン)を持つタンパク質(HBD1)が、DNAクリップとしてDNAを折り曲げ、架橋することでDNAを折りたたみ、核様体を構築していることが示された。ここで得られた知見は葉緑体工学における葉緑体ゲノムの安定性や遺伝子発現制御に関する新技術開発、さらにヒトを含む動物・植物におけるミトコンドリア核様体の機能解析への応用、医学・農学をふくむ様々な分野への展開が期待される。
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Report
(4 results)
Research Products
(41 results)
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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)
Kayoko Yamamoto, Takashi Hamaji, Hiroko Kawai-Toyooka, Ryo Matsuzaki, Fumio Takahashi, Yoshiki Nishimura, Masanobu Kawachi, Hideki Noguchi, Yohei Minakuchi, James G. Umen, Atsushi Toyoda, Hisayoshi Nozaki
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Journal Title
The Proceedings of the National Academy of Sciences
Volume: 118
Issue: 21
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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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
Related Report
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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