Molecular mechanisms on the replication initiation which leads to loading of the helicase and the regulatory systems for the replication initiation
| Project/Area Number |
17H03656
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
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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 |
¥17,420,000 (Direct Cost: ¥13,400,000、Indirect Cost: ¥4,020,000)
Fiscal Year 2019: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2018: ¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2017: ¥6,240,000 (Direct Cost: ¥4,800,000、Indirect Cost: ¥1,440,000)
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| Keywords | DNA複製開始 / 高次複合体 / 試験管内再構成系 / 蛋白質 / 細菌 / 遺伝子 / 分子機械 / AAA+ファミリー / DNA複製 / ゲノム / タンパク質 / 複合体動態 / 核酸 |
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| Outline of Final Research Achievements |
The replication initiation complex in E. coli consists of the origin DNA, the initiator protein DnaA, the DNA-bending protein IHF and so on. This complex promotes unwinding of the origin DNA and loading of the replicative helicase DnaB to the unwound DNA region. In the research #1 “Analysis of loading mechanism of DnaB helicase to the origin DNA”, I mainly revealed the molecular mechanism of the unwinding of origin DNA by DnaA and the interaction mechanism between DnaA and DnaB. Also, in the research #2 “Analysis of functional mechanisms of the regulatory systems for DnaA”, I mainly revealed dynamic mechanism of DnaA complex formed in the DARS system which activates DnaA in a timely manner during the cell cycle.
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| Academic Significance and Societal Importance of the Research Achievements |
複製起点DNAの一本鎖化と複製へリカーゼの一本鎖DNAへの導入は、染色体DNAの複製開始における共通機構と言える。それらにおける主要機構を解明したことには、大腸菌のみならず、細胞増殖の原則的な分子動態を理解するために高い学術的意義がある。さらにDnaAを適時的に活性化する主要な分子機構を解明したことにも、細菌の増殖における原理的な分子機構を理解するために高い学術的意義がある。特にこの成果は独創性も高く、国際的な学術専門家団体(F1000Prime)からも高く評価された。さらに抗菌剤等の新たな医薬品開発の基盤としても発展性をもつものといえる。
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Report
(4 results)
Research Products
(67 results)
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[Journal Article] Crystal structure of the complex of the interaction domains of E. coli DnaB helicase and DnaC helicase loader: Structural basis implying a distortion-accumulation mechanism for the DnaB ring opening caused by DnaC binding2020
Author(s)
Nagata, K., Okada, A., Ohtsuka, J., Ohkuri, T., Akama, Y., Sakiyama, Y., Miyazaki, E., Horita, S., Katayama, T., Ueda, T., and Tanokura, M.
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Journal Title
J. Biochem.
Volume: 167
Issue: 1
Pages: 1-14
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] A novel mode of DnaA-DnaA interaction promotes ADP dissociation for reactivation of replication initiation activity2019
Author(s)
Sugiyama, R., Kasho, K., Miyoshi, K., Ozaki, S., Kagawa, W., Kurumizaka, H., and Katayama, T
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Journal Title
Nucleic Acids Res.
Volume: 47
Issue: 21
Pages: 11209-11224
DOI
Related Report
Peer Reviewed / Open Access
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[Presentation] Dynamic mechanisms of higher-order complexes for replication initiation and regulation of the E. coli genome2019
Author(s)
Tsutomu Katayama, Kenya Miyoshi, Chihiro Hayashi, Ryusei Yoshida, Ryo Sugiyama, Ryuji Sakai, Yukari Sakiyama, Kazutoshi Kasho, Hironori Kawakami, Shogo Ozaki, Mariko Nagata
Organizer
第92回日本生化学会大会 シンポジウム「新しいゲノムの姿とその維持機構のフレキシビリティ」
Related Report
Int'l Joint Research
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[Presentation] Single-stranded DNA binding of replication initiator in budding yeast2019
Author(s)
Kawakami, H., Muraoka, R., Kurihara, T., Chichibu, T., Kanamoto, S., Kawabata, K., Ohashi, E., Tsurimoto, T., Katayama, T.
Organizer
第42回日本分子生物学会年会 Workshop "New Frontiers in Studies of DNA Replication"
Related Report
Int'l Joint Research
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[Presentation] ssDNA as a dynamic and genome-wide mediator governing specificity of eukaryotic replication origin selection2018
Author(s)
Hironori Kawakami, Takeaki Chichibu, Shota Kanamoto, Takuya Kurihara, Ryuya Muraoka, Eiji Ohashi, Toshiki Tsurimoto, Tsutomu Katayama
Organizer
The 11th 3R(Replication, Repair, Recombination)+3C(Chromosome, Chromatin, Cell cycle) Sympojium
Related Report
Int'l Joint Research
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