Fluorescence Polarization Analysis for Revealing Molecular Mechanism of Nucleotide-Dependent Phospholipid Membrane Binding of MinD Adenosine 5′-Triphosphate, Adenosine Triphosphatase
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概要
- 論文の詳細を見る
Membrane binding of Walker type adenosine 5′-triphosphate, adenosine triphosphatase (ATPase), MinD, is a key step in regulating the site of cell division in Escherichia coli. Two lysine residues (K11, K16) in the Walker A motif of MinD have been suggested to be essential for both membrane binding and ATPase activity, but the relationship between the membrane binding of MinD and its ATPase activity is still unclear. To reveal the role of K11 and K16 in MinD membrane interaction and ATP-binding, we compared the functionality of wild-type MinD (WT) and two MinD mutants that lack ATPase activity, where alanine was substituted for lysine at positions 11 and 16 (K11A, K16A), using liposomes and fluorescent-labeled ATP. The ATP dissociation constant (Kd) of wild-type MinD was 4.9 μM. Unexpectedly, the Kd values of the two lysine mutants were almost the same as that of wild type, indicating that ATP can bind to MinD mutants, even though these mutants showed no ATPase activity and membrane binding ability. Our results presumed that K11 and K16 residues might play an important role in dimmer formation of MinD, but not ATP binding step, for recruiting to membrane.
- 公益社団法人 日本薬学会の論文
著者
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Funasaki Noriaki
Department of Physical Chemsitry, Kyoto Pharmaceutical University
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Okuno T
Graduate School Of Medicine And Pharmaceutical Sciences Univ. Of Toyama
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Kogure Kentaro
Department Of Biophysical Chemistry Kyoto Pharmaceutical University
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Okuno Takashi
Graduate School of Medicine and Pharmaceutical Sciences, University of Toyama
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Okuno Takashi
Graduate School Of Medicine And Pharmaceutical Sciences University Of Toyama
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Funasaki Noriaki
Department Of Physical Chemistry 21st Century Coe Program Kyoto Pharmaceutical University
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Ohgita Takashi
Department of Biophysical Chemistry, Kyoto Pharmaceutical University
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Sasa Tatsunori
Department of Biophysical Chemistry, Kyoto Pharmaceutical University
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Nonaka Aoi
Department of Biophysical Chemistry, Kyoto Pharmaceutical University
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Sasa Tatsunori
Kyoto Pharmaceutical University
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Funasaki Noriaki
Department of Biophysical Chemistry, Kyoto Pharmaceutical University
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