Structural basis of replication restart primosome proteins involved in DnaB helicase loading
Project/Area Number |
23570140
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Structural biochemistry
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Research Institution | Kyushu University |
Principal Investigator |
ABE Yoshito 九州大学, 薬学研究科(研究院), 准教授 (60315091)
|
Co-Investigator(Kenkyū-buntansha) |
KATAYAMA Tsutomu 九州大学, 大学院薬学研究院, 教授 (70264059)
|
Project Period (FY) |
2011 – 2013
|
Project Status |
Completed (Fiscal Year 2013)
|
Budget Amount *help |
¥5,330,000 (Direct Cost: ¥4,100,000、Indirect Cost: ¥1,230,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2011: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
Keywords | 複製再開始プライモソーム / タンパク質-DNA複合体 / タンパク質構造 / DnaT / PriC / 複製再開始 / PriB / 複製開始プライモソーム / 蛋白質-DNA複合体 / 蛋白質構造 |
Research Abstract |
We performed the structure and function analysis of PriB, DnaT and PriC proteins engaged in replication restart in Escherichia coli. PriB is a single-stranded DNA (ssDNA) binding protein. Our NMR and FRET results showed that PriB bound to ssDNA in two-step binding manner, suggesting the cooperative binding between PriB and ssDNA. We also performed domain analysis of DnaT and PriC. From the domain information of DnaT, we suggested that the N-terminal domain of DnaT was involved in trimer formation and interaction with PriB, and the C-terminal domain of DnaT was involved in ssDNA binding based on the structure determined by NMR analysis. Furthermore, the domain information of PriC suggested that the C-terminal domain of PriC was involved in the ssDNA and SSB (single-stranded DNA binding protein) binding. Additionally, we determined the N-terminal domain of PriC using NMR analysis. Together with these results, we proposed the model of replication restart in Escherichia coli.
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Report
(4 results)
Research Products
(37 results)
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[Journal Article] Involvement of histidine in complex formation of PriB and single-stranded DNA2014
Author(s)
Fujiyama, S, Abe, Y, Takenawa, T, Aramaki, T, Shioi, S, Katayama, T & Ueda, T
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Journal Title
Biochim Biophys Acta
Volume: 1844
Pages: 299-307
Related Report
Peer Reviewed
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[Journal Article] Domain separation and characterization of PriC, a replication restart primosome factor in Escherichia coli2013
Author(s)
Aramaki, T, Abe, Y, Ohkuri, T, Mishima, T, Yamashita, S, Katayama, T & Ueda, T
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Journal Title
Genes Cells
Volume: 18
Pages: 723-732
Related Report
Peer Reviewed
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[Journal Article] The DnaA N-terminal domain interacts with Hda to facilitate replicase clamp-mediated inactivation of DnaA2013
Author(s)
Su'etsugu, M, Harada, Y, Keyamura, K, Matsunaga, C, Kasho, K, Abe, Y, Ueda, T & Katayama, T
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Journal Title
Environ Microbiol
Volume: 15
Pages: 3183-3195
Related Report
Peer Reviewed
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[Journal Article] The DnaA N-terminal domain interacts with Hda to facilitate replicase clamp-mediated inactivation of DnaA2013
Author(s)
Su'etsugu, M., Harada, Y., Keyamura, K., Matsunaga, C., Kasho, K., Abe, Y., Ueda, T. and Katayama, T.
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Journal Title
nviron. Microbiol.
Volume: (印刷中)
Issue: 12
Pages: 3183-3195
DOI
Related Report
Peer Reviewed
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[Journal Article] Preparation and characterization of a monoclonal antibody against the refolded and functional extracellular domain of rat P2X4 receptor.2013
Author(s)
Igawa, T., Higashi, S., Abe, Y., Ohkuri, T., Tanaka, H., Morimoto, S., Yamashita, T., Tsuda, M., Inoue K., Ueda, T.
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Journal Title
Journal of Biochemistry,
Volume: 153(3)
Issue: 3
Pages: 275-82
DOI
Related Report
Peer Reviewed
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