Functional analysis based on the structure of DNA replication proteins in Escherichia coli
| Project/Area Number |
18570110
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Structural biochemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
ABE Yoshito Kyushu University, Facuky of Pharmaceutical Science, Associate Professor (60315091)
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| Co-Investigator(Kenkyū-buntansha) |
KATAYAMA Tsutomu Kyushu University, Faculty of Pharmaceutical Science, Professor (70264059)
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| Project Period (FY) |
2006 – 2007
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| Project Status |
Completed (Fiscal Year 2007)
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| Budget Amount *help |
¥4,110,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥510,000)
Fiscal Year 2007: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
Fiscal Year 2006: ¥1,900,000 (Direct Cost: ¥1,900,000)
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| Keywords | DNA replication / NMR / Protein structure / Protein-protein interaction / Protein complex / 複製開始因子 / タンパク質間相互作用 / NMR解析 / タンパク質構造 / タンパク質複合体 |
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| Research Abstract |
Based on the structure, we examined the functions of proteins which were associated with DNA replication initiation. Firstly, we examined the N-terminal domain of DnaA. DnaA protein is a key protein in the initiation of chromosomal replication in Escherichia coli. The structure of E. coli DnaA is subdivided into four functional domains. Although the structure of domain III and IV were already determined, the structure of N-terminal domain, which contains DnaA oligomerization activity and DnaB helicase binding sites, was not understood. To determined the structure of N-terminal domain, we assigned the ^1H,^<13>C and ^<15>N backbone resonances of N-terminal domain of Dna A (Bio NMR assignment 2007). Furthermore, we determined the N-terminal domains (1-108) structure using NMR spectroscopic method. Domain I has an α-α-β-β-α-β motif, similar to that of the K homology (KH) domain and has weak affinity for oriC single-stranded DNA, consistent with KH domain function. A hydrophobic surface carrying Trp-6 most likely forms the interface for domain I dimerization. Glu-21 is located on the opposite surface of domain I from the Trp-6 site and is crucial for DnaB helicase loading. These findings suggested a model for DnaA homomultimer formation and DnaB helicase loading on oriC (J. Biol. Chem. 2007) . This paper was selected as Papers of the Week in J. Biol. Chem. 2007, June 15. And then, we examined the protein functional and structural analyses of heat shock protein HSPQ associated with DnaA degradation, cell division re-activator CedA, and the primosome component PriB. Some part of these results was announced at the several academic conferences.
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Report
(3 results)
Research Products
(29 results)
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[Journal Article] Structure and function of DnaA N-terminal domains : specific sites and mechanisms in inter-DnaA interaction and in DnaB helicase loading on oriC2007
Author(s)
Abe, Y., Jo, T., Matsuda, Y., Matsunaga, C., Katayama, T., Ueda, T
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Journal Title
Journal of biological chemistry 282
Pages: 17816-27
Description
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[Journal Article] Assignment of ^1H,^<13>C and ^<15>N resonances of N-terminal Domain of DnaA protein.2007
Author(s)
Abe, Y., Watanabe, N., Yoshida, Y., Ebata, F., Katayama, T., Ueda, T
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Journal Title
Biomolecular NMR assignment 1
Pages: 57-9
Description
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[Journal Article] Crystal Structure of Tapes japonica Lysozyme with Substrate Analogue : STRUCTURAL BASIS OF THE CATALYTIC MECHANISM AND MANIFESTATION OF ITS CHITINASE ACTIVITY ACCOMPANIED BY QUATERNARY STRUCTURAL CHANGE2007
Author(s)
Goto, T., Abe, Y., Kakuta, Y., Takeshita, K., Imoto, T., Ueda, T
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Journal Title
Journal of biological chemistry 282
Pages: 27459-67
Description
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[Journal Article] Identification of oxidized methionine sites in erythrocyte membrane protein using LC/ESI MS peptide mapping2006
Author(s)
Li, C., Takazaki, S., Jin, X., Kang, D., Abe, Y., Hamasaki, N
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Journal Title
Biochemistry 45
Pages: 12117-124
Description
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[Journal Article] A simple search of TM segments in polytopic membrane protein using matrix-assisted laser desorption ionization time-of-flight mass spectrometry2006
Author(s)
Abe, Y., Hamasaki, T., Turusaki, S., Takazaki, S., Jin, X., Kang, D., Hamasaki, N
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Journal Title
Protein & Peptide Letters 13
Pages: 761-67
Description
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[Presentation] Structure and function analysis of DNA binding to CedA, cell division reactivater2006
Author(s)
Abe, Y., Watanabe, N., Matsuda, Y., Yoshida, Y., Katayama, T., Ueda, T
Organizer
Biomedical Analytical Science Symposium
Place of Presentation
Fukuoka
Year and Date
2006-08-02
Description
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[Presentation] Structural Analysis and Molecular Interaction of a Cell Division Reactivation Factor, CedA, from Escherichia coli2006
Author(s)
Abe, Y., Watanabe, N., Matsuda, Y., Yoshida, Y., Katayama, T., Ueda, T
Organizer
20th IUBMB International Congress of Biochemistry and Molecular Biology and 11th FAOBMB Congress
Place of Presentation
Kyoto
Year and Date
2006-06-22
Description
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[Presentation] NMR analysis of the interaction between single stranded DNA and PriB, the Primosome component2006
Author(s)
Takenawa, T., Shioi, S., Abe, Y., Katayama, T., Ueda, T
Organizer
Japan Biochemical Society Kyushu Branch
Place of Presentation
Fukuoka
Year and Date
2006-05-21
Description
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