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Proceedings Paper

Regulatory conformational changes of the epsilon subunit in single FRET-labeled FoF1-ATP synthase
Author(s): Thomas M. Duncan; Monika G. Düser; Thomas Heitkamp; Duncan G. G. McMillan; Michael Börsch
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Paper Abstract

Subunit ε is an intrinsic regulator of the bacterial FoF1-ATP synthase, the ubiquitous membrane-embedded enzyme that utilizes a proton motive force in most organisms to synthesize adenosine triphosphate (ATP). The C-terminal domain of ε can extend into the central cavity formed by the α and β subunits, as revealed by the recent X-ray structure of the F1 portion of the Escherichia coli enzyme. This insertion blocks the rotation of the central γ subunit and, thereby, prevents wasteful ATP hydrolysis. Here we aim to develop an experimental system that can reveal conditions under which ε inhibits the holoenzyme FoF1-ATP synthase in vitro. Labeling the C-terminal domain of ε and the γ subunit specifically with two different fluorophores for single-molecule Förster resonance energy transfer (smFRET) allowed monitoring of the conformation of ε in the reconstituted enzyme in real time. New mutants were made for future three-color smFRET experiments to unravel the details of regulatory conformational changes in ε.

Paper Details

Date Published: 28 February 2014
PDF: 15 pages
Proc. SPIE 8948, Multiphoton Microscopy in the Biomedical Sciences XIV, 89481J (28 February 2014); doi: 10.1117/12.2040463
Show Author Affiliations
Thomas M. Duncan, SUNY Upstate Medical Univ. (United States)
Monika G. Düser, Univ. Stuttgart (Germany)
Thomas Heitkamp, Friedrich-Schiller-Univ. Jena (Germany)
Duncan G. G. McMillan, Friedrich-Schiller-Univ. Jena (Germany)
Michael Börsch, Friedrich-Schiller-Univ. Jena (Germany)


Published in SPIE Proceedings Vol. 8948:
Multiphoton Microscopy in the Biomedical Sciences XIV
Ammasi Periasamy; Peter T. C. So; Karsten König, Editor(s)

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