The c15 ring of the Spirulina platensis F-ATP synthase: F1/F0 symmetry mismatch is not obligatory.
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.
Pogoryelov
Denys
D
Institute of Microbiology, Eidgenössische Technische Hochschule, Wolfgang-Pauli Strasse 10, Zurich 8093, Switzerland.
Yu
Jinshu
J
Meier
Thomas
T
Vonck
Janet
J
Dimroth
Peter
P
Muller
Daniel J
DJ
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
D021122:Protein Subunits; D006180:Proton-Translocating ATPases