Characterization of FtsZ Homolog from Hyperthermophilic Archaeon Pyrococcus kodakaraensis KOD1
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概要
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The gene of bacterial type ftsZ homolog in hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1 (Pk-ftsZ), was identified. The gene product of the Pk-ftsZ gene is composed of 380 amino acids with a molecular mass of 41, 354 Da. In the deduced amino acid sequence of the Pk-ftsZ gene, a glycine-rich sequence (Gly-Gly-Gly-Thr-Gly-Ala-Gly) implicated in GTP binding was well conserved. The Pk-ftsZ gene was overexpressed using Escherichia coli as a host and the recombinant protein was purified. The purified Pk-FtsZ protein exhibited GTPase activity with optimum temperatures higher than 80℃. However, the protein showed little GTPase activity at 40℃, indicating that a high reaction temperature is required for the GTPase activity in accordance with the thermophilic nature of P.kodakaraensis KOD1. The GTP-binding ability of Pk-FtsZ protein could also be detected by UV-induced cross-linking of a protein to [α-^<32>P] GTP. The Pk-ftsZ gene was expressed in E.coli cells with a temperature-sensitive ftsZ mutation, E.coli ftsZ84(ts), but its mutant phenotype of elongated cell form at a nonpermissive temperature(42℃) could not be compensated, possibly because of the thermophilic nature of the Pk-FtsZ. Pk-FtsZ could form protofilaments in a GTP-dependent manner at 90℃. Results of phylogenetic analysis suggest that there might be additional factors required for formation of the Z ring in P.kodakaraensis KOD1.
- 社団法人日本生物工学会の論文
- 2000-02-25
著者
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Takagi Masahiro
School Of Materials Science Japan Advanced Institute Of Science And Technology
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Takagi M
School Of Materials Science Japan Advanced Institute Of Science And Technology
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Takagi Mutsumi
International Center For Biotechnology Osaka University:(present Address)division Of Biotechnology A
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FUJIWARA SHINSUKE
Department of Bioscience, School of Science and Technology, Kwansei Gakuin University
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Nakamura Tsuyoshi
Department of Nutrition and Health Science, Fukuoka Women’s University
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IMANAKA Tadayuki
Department of Synthetic and Biological Chemistry, Graduate School of Engineering, Kyoto University
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TAKAGI MASAHIRO
Department of Biotechnology, Graduate School of Engineering, Osaka University
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Fujiwara S
School Of Science And Engineering Department Of Life Science Kwansei-gakuin University
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Fujiwara Shinsuke
Department Of Biotechnology Graduate School Of Engineering Osaka University
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Fujiwara Shinsuke
Department Of Bioscience School Of Science And Technology Kwansei Gakuin University
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NAGAHISA KEISUKE
Department of Biotechnology, Graduate School of Engineering, Osaka University
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Takagi M
Nagasaki Univ. Nagasaki Jpn
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Imanaka Tadayuki
Department Of Applied Biotechnology Faculty Of Engineering Osaka University
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Fujiwara Shinsuke
School Of Science And Engineering Department Of Life Science Kwansei-gakuin University
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Nagahisa Keisuke
Department Of Bioinformatic Engineering Graduate School Of Information Science And Technology Osaka
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Nagahisa K
Osaka Univ. Osaka Jpn
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Imanaka T
Dep. Of Biotechnology Coll. Of Life Sciences Ritsumeikan Univ.
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Takagi Masahiro
Graduate School Of Biological Sciences Nara Institute Of Science And Technology (naist)
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Nakamura Tsuyoshi
Department Of Biotechnology Graduate School Of Engineering Osaka University
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Nakamura Tsuyoshi
Department Of Applied Physics Fukui University
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Takagi Masahiro
Department Of Biotechnology Faculty Of Engineering Osaka University
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Fujiwara Shinsuke
Department Of Bioscience Graduate School Of Science And Technology Kwansei-gakuin University:researc
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