title: The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory.
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.
authors.affiliation: Institute of Microbiology, Eidgenössische Technische Hochschule, Wolfgang-Pauli Strasse 10, Zurich 8093, Switzerland.
authors.forename: Denys
authors.initials: D
authors.lastname: Pogoryelov
authors.forename: Jinshu
authors.initials: J
authors.lastname: Yu
authors.forename: Thomas
authors.initials: T
authors.lastname: Meier
authors.forename: Janet
authors.initials: J
authors.lastname: Vonck
authors.forename: Peter
authors.initials: P
authors.lastname: Dimroth
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Muller
mesh_terms: D003460:Crystallization; D000458:Cyanobacteria / Q000201:enzymology*; D013058:Mass Spectrometry; D018625:Microscopy, Atomic Force; D021122:Protein Subunits / Q000737:chemistry; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D021122:Protein Subunits; D006180:Proton-Translocating ATPases