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EMBO reports 6, 11, 1040–1044 (2005)
doi:10.1038/sj.embor.7400517
Published online: 9 September 2005
The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory
Denys Pogoryelov1, Jinshu Yu2, Thomas Meier1, Janet Vonck3, Peter Dimroth1 & Daniel J Muller2
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1 Institute of Microbiology, Eidgenössische Technische Hochschule, Wolfgang-Pauli Strasse 10, Zurich 8093, Switzerland
2 Department of Cellular Machines, Centre for Biotechnology, University of Technology, Tatzberg 47, Dresden 01307, Germany
3 Department of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue Strasse 3, Frankfurt am Main 60438, Germany
To whom correspondence should be addressed
Thomas Meier Tel: +41 44 6325523; Fax: +41 44 6321378; E-mail: meier@micro.biol.ethz.ch
Daniel J Muller Tel: +49 351 46340330; Fax: +49 351 46340342; E-mail: mueller@biotec.tu-dresden.de
Received 2 May 2005; Accepted 3 August 2005; Published online 9 September 2005.
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Abstract
The oligomeric c ring of the F-ATP synthase from the alkaliphilic cyanobacterium Spirulina platensis was isolated and characterized. Mass spectroscopy analysis indicated a mass of 8,210 Da, reflecting that of a c monomer. The mass increased by 206 Da after treatment with the c-subunit-specific inhibitor dicyclohexylcarbodiimide (DCCD), which indicated modification of the ion-binding carboxylate by DCCD. Atomic force microscopy topographs of c rings from S. platensis showed 15 symmetrically assembled subunits. The c15-mer reported here is the largest c ring that is isolated and does not show the classical c-ring mismatch to the three-fold symmetry of the F1 domain.
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