The Oligomeric State of c Rings from Cyanobacterial F-ATP Synthases Varies from 13 to 15
- 15 August 2007
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 189 (16), 5895-5902
- https://doi.org/10.1128/jb.00581-07
Abstract
We isolated the c rings of F-ATP synthases from eight cyanobacterial strains belonging to four different taxonomic classes (Chroococcales, Nostocales, Oscillatoriales, and Gloeobacteria). These c rings showed different mobilities on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), probably reflecting their molecular masses. This supposition was validated with the previously characterized c(11), c(14), and c(15) rings, which migrated on SDS-PAGE in proportion to their molecular masses. Hence, the masses of the cyanobacterial c rings can conveniently be deduced from their electrophoretic mobilities and, together with the masses of the c monomers, allow the calculation of the c ring stoichiometries. The method is a simple and fast way to determine stoichiometries of SDS-stable c rings and hence a convenient means to unambiguously determine the ion-to-ATP ratio, a parameter reflecting the bioenergetic efficacy of F-ATP synthases. AFM imaging was used to prove the accuracy of the method and confirmed that the c ring of Synechococcus elongatus SAG 89.79 is a tridecameric oligomer. Despite the high conservation of the c-subunit sequences from cyanobacterial strains from various environmental groups, the stoichiometries of their c rings varied between c(13) and c(15). This systematic study of the c-ring stoichiometries suggests that variability of c-ring sizes might represent an adaptation of the individual cyanobacterial species to their particular environmental and physiological conditions. Furthermore, the two new examples of c(15) rings underline once more that an F(1)/F(o) symmetry mismatch is not an obligatory feature of all F-ATP synthases.Keywords
This publication has 45 references indexed in Scilit:
- Structural Investigations of the Membrane-Embedded Rotor Ring of the F-ATPase from Clostridium paradoxumJournal of Bacteriology, 2006
- Structural evidence for a constant c11 ring stoichiometry in the sodium F‐ATP synthaseThe FEBS Journal, 2005
- The stoichiometry of the chloroplast ATP synthase oligomer III in Chlamydomonas reinhardtii is not affected by the metabolic stateBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2004
- Self‐assembly of ATP synthase subunit c ringsFEBS Letters, 2002
- Membrane Topography of the Coupling Ion Binding Site in Na+-translocating F1F0 ATP SynthasePublished by Elsevier ,2002
- Molecular Architecture of the Rotary Motor in ATP SynthaseScience, 1999
- The H+/ATP coupling ratio of the ATP synthase from thiol‐modulated chloroplasts and two cyanobacterial strains is fourFEBS Letters, 1996
- Effects of the uncI gene on expression of uncB, the gene coding for the a subunit of the F1F0 ATPase of Escherichia coliFEBS Letters, 1995
- Subunit III of the chloroplast ATP-synthase can form a Ca2+-binding site on the lumenal side of the thylakoid membraneFEBS Letters, 1993
- Proton Gradients in Intact CyanobacteriaPlant Physiology, 1987