Structural-functional analysis of the radiation-inducible protein DdrA and its paralog DdrAP
| Project/Area Number |
17K07730
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Applied microbiology
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| Research Institution | Toyo University |
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Principal Investigator |
Narumi Issay 東洋大学, 生命科学部, 教授 (90343920)
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| Project Period (FY) |
2017-04-01 – 2020-03-31
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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2019: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2018: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2017: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | DNA修復 / 放射線抵抗性細菌 / DNA損傷誘導性 / ゲノム2本鎖切断修復 / DAN損傷誘導性 / DNA修復タンパク質 / 放射線誘導性タンパク質 |
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| Outline of Final Research Achievements |
The functional analyses of radiation-inducible protein DdrA and its paralog protein DdrAP from the radioresistant bacterium were carried out especially in terms of DNA repair. The ddrA deletion mutant showed a sensitivity to nalidixic acid. On the other hand, the ddrAP deletion mutant showed a resistance to novobiocin. These results suggest that DdrA and DdrAP proteins interact with the GyrA and GyrB subunits of topoisomerase, respectively, thereby, the interaction triggers a conformational change in topoisomerase, and changes the effects of topoisomerase inhibitors. The in vivo experiment using Western blot analysis and in vitro experiment using purified recombinant proteins revealed that a certain DdrA-degradative enzyme exists in crude cell extracts from the radioresistant bacterium, and it was suggested that DdrA protein avoids the cleavage activity of the DdrA-degradative enzyme by forming a heterocomplex with DdrAP protein.
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| Academic Significance and Societal Importance of the Research Achievements |
放射線抵抗性細菌に特有のDNA修復機構である凝縮核様体依存性末端結合の構成要素としてこれまでに、PprAタンパク質、DNAトポイソメラーゼ、DNAリガーゼが明らかになっている。本研究によって、DdrAタンパク質及びDdrAPタンパク質は、DNAトポイソメラーゼと相互作用することが示唆され、CNDEJの構成要素として放射線抵抗性細菌が持つDNA損傷誘導性のDNA修復機構の一端を担うことが明らかになった。これらの構成要素の相互作用の詳細が明らかになれば、それらの相互作用を利用した新たな遺伝子工学試薬の開発にも繋がり、生命科学の新たな展開に貢献すると考えられる。
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Report
(4 results)
Research Products
(57 results)
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[Journal Article] Pol B, a Family B DNA Polymerase, in <i>Thermococcus kodakarensis</i> is Important for DNA Repair, but not DNA Replication2019
Author(s)
Takashi Kushida, Issay Narumi, Sonoko Ishino, Yoshizumi Ishino, Shinsuke Fujiwara, Tadayuki Imanaka, Hiroki Higashibata
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Journal Title
Microbes and Environments
Volume: 34
Issue: 3
Pages: 316-326
DOI
NAID
ISSN
1342-6311, 1347-4405
Related Report
Peer Reviewed / Open Access
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[Journal Article] Enlargement of Deinococcus grandis spheroplasts requires Mg2+ or Ca2+2018
Author(s)
Koki Nishino, Yusuke Morita, Sawako Takahashi, Mai Okumura, Shusaku Shiratani, Kousuke Umemura, Issay Narumi, Chie Kondo, Ryosuke Ochiai, Taku Oshima, Hiromi Nishida
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Journal Title
Microbiology
Volume: 164
Issue: 11
Pages: 1361-1371
DOI
Related Report
Peer Reviewed / Open Access
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[Presentation] Survival and DNA damage of deinococcal species in space: three years of microbe space exposure experiment of Tanpopo mission at Exposure Facility of Japanese Experiment Module of International Space Station2019
Author(s)
Shin-ichi Yokobori, Yuko Kawaguchi, Jun Yatabe, Daisuke Fujiwara, Risako Hayashi, Iori Kinoshita, Yuka Murano, Mio Shibuya, Issay Narumi, Hirofumi Hashimoto, Akihiko Yamagishi
Organizer
European Astrobiology Network Association Conference (EANA 2019)
Related Report
Int'l Joint Research
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[Presentation] Survival and DNA damage of cell-aggregate of Deinococcus spp. exposed in space for two-years2018
Author(s)
Yuko Kawaguchi, Mio Shibuya, Iori Kinoshita, Risako Hayashi, Jun Yatabe, Daisuke Fujiwara, Issay Narumi, Yuka Murano, Hirofumi Hashimoto, Shin-ichi Yokobori, Akihiko Yamagishi
Organizer
42nd Committee on Space Research Scientific Assembly (COSPAR 2018)
Related Report
Int'l Joint Research
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