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J. Biol. Chem., Vol. 277, Issue 23, 20117-20119, June 7, 2002

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ACCELERATED PUBLICATION
Substitution of a Single Amino Acid Switches the Tentoxin-resistant Thermophilic F₁-ATPase into a Tentoxin-sensitive Enzyme^*

Georg Groth, Toru Hisabori^§¶, Holger Lill, and Dirk Bald^**

From the  Department of Plant Biochemistry, Heinrich-Heine Universitat, D-40225 Dusseldorf, Germany, the ^§ Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Midori-ku, Yokohama 226-8503, Japan, the ^¶ Yoshida ATP System Project, Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Corporation (JST), 5800-3 Nagatsuta-cho, Midori-ku, Yokohama 226-0026, Japan, and the  Department of Structural Biology, Faculty of Earth and Life Science, Vrije Universiteit Amsterdam, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands

In contrast to the homologous bacterial and mitochondrial enzymes the chloroplast F₁-ATPase (CF₁) is strongly affected by the phytopathogenic inhibitor tentoxin. Based on structural information obtained from crystals of a CF₁-tentoxin co-complex (Groth, G. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 3464-3468) we have replaced residues Ser⁶⁶ and Arg¹³² in the ₃₃ subcomplex of the thermophilic F₁-ATPase from Bacillus PS3 by the corresponding residues of the chloroplast ATPase to confer tentoxin sensitivity to the thermophilic enzyme. The mutation Arg¹³²  Pro, proposed to relieve steric constraints on tentoxin binding, did not have any significant effect. However, mutation Ser⁶⁶  Ala, predicted to provide a crucial hydrogen bond with the inhibitor, resulted in tentoxin inhibition of ATP hydrolysis comparable with the situation found with the chloroplast enzyme.

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