1998 Fiscal Year Final Research Report Summary
Molecular evolution of recombinational mechanism
| Project/Area Number |
09044223
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| Research Category |
Grant-in-Aid for international Scientific Research
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| Allocation Type | Single-year Grants |
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| Section | Joint Research |
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| Research Field |
Molecular biology
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| Research Institution | Osaka University |
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Principal Investigator |
KURAMITSU Seiki Graduate School of Science, Professor, 大学院・理学研究科, 教授 (60153368)
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| Co-Investigator(Kenkyū-buntansha) |
DOMITRI Baitin Petersburn Nuclear Physics Institue of the Academy Associae Researcher, 研究員
KIL Yuri V. Petersburg Nuclear Physics Institue of the Academy, Associate Researcher, 研究員
LANZOV Vladi ペテルブルグ核物理学研究所, 部長
HIROTSU Ken Graduate School of Science Osaka city university, Professor, 理学部, 教授 (10047269)
OHSHIMA Toshihisa Faculty of engineering Tokushima univesity, Professor, 工学部, 教授 (10093345)
LANZOV Vladislav A. Petersburg Nuclear Physics Institue of the Academy, Head
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| Project Period (FY) |
1997 – 1998
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| Keywords | thermophilic bacteria / archea / recA gene / recombinational mechanism / cloning / gene analysis / enzyme reaction mechanism / molecular evolution |
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| Research Abstract |
The RecA protein plays the central role in the process of genetic recombination and is highly conserved in most living organisms. The RecA-like recombinational proteins are involved in genetic recombination and DNA replication, but the structure and function relationship is still uncertain. In order to elucidate the relationship among evolutionary divergent RecA-like proteins of archea, prokaryotes and eukaryotes, we cloned their RecA homologes.
The recA/RAD51 gene of thermophilic bacteria had cloned common central regions. They showed DNA strand-exchange activities and DNA-dependent ATPase activities, which are essential properties of homologous recombination. Some thermophilic RecA proteins could be crystallized with and without DNA.Some RadA protein exhibited a break in the Arrhenius plot of ATP hydrolysis at 75ﾟC.The coperativity of ATP hydrolysis and single-stranded DNA binding ability of the protein above 75ﾟC were larger than those at lower temperatures, while the activation energy of ATP hydrolysis was lower above this break point temperature. These results suggest that this hyperthermophilic RadA exists in two different conformations, with 75ﾟC being the critical temperature.
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[Publications] Alexseyev, A.A., Baitin, D.M., Kuramitsu, S., Ogawa, T., Ogawa, H., and Lanzov, V.A.: "A Recombinational Defect in the C-Terminal Domain of Escherichia coli RecA2278-5 Protein is Compensated by Protein Binding to ATP" Mol.Microbiology. 23(2). 255-265 (1997)
Description
「研究成果報告書概要(欧文)」より
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