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Subunit epsilon is an intrinsic regulator of the bacterial FoF1-ATP synthase,the ubiquitous membrane-embedded enzyme that utilizes a proton motive force inmost organisms to synthesize adenosine triphosphate (ATP). The C-terminaldomain of epsilon can extend into the central cavity formed by the alpha andbeta subunits, as revealed by the recent X-ray structure of the F1 portion ofthe Escherichia coli enzyme. This insertion blocks the rotation of the centralgamma subunit and, thereby, prevents wasteful ATP hydrolysis. Here we aim todevelop an experimental system that can reveal conditions under which epsiloninhibits the holoenzyme FoF1-ATP synthase in vitro. Labeling the C-terminaldomain of epsilon and the gamma subunit specifically with two differentfluorophores for single-molecule Foerster resonance energy transfer (smFRET)allowed monitoring of the conformation of epsilon in the reconstituted enzymein real time. New mutants were made for future three-color smFRET experimentsto unravel the details of regulatory conformational changes in epsilon.

Regulatory conformational changes of the epsilon subunit in single FRET-labeled FoF1-ATP synthase