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Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases

1
Single-Molecule Microscopy Group, Jena University Hospital, Friedrich Schiller University, 07743 Jena, Germany
2
School of Life Sciences, Arizona State University, Tempe, Arizona, AZ 85287, USA
3
Department of Biology & Chemistry, University of Osnabrück, 49076 Osnabrück, Germany
*
Author to whom correspondence should be addressed.
Molecules 2019, 24(3), 504; https://doi.org/10.3390/molecules24030504
Received: 13 December 2018 / Revised: 23 January 2019 / Accepted: 29 January 2019 / Published: 30 January 2019
(This article belongs to the Special Issue Single-Molecule Fluorescence Spectroscopy)
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Abstract

F-ATP synthases use proton flow through the FO domain to synthesize ATP in the F1 domain. In Escherichia coli, the enzyme consists of rotor subunits γεc10 and stator subunits (αβ)3δab2. Subunits c10 or (αβ)3 alone are rotationally symmetric. However, symmetry is broken by the b2 homodimer, which together with subunit δa, forms a single eccentric stalk connecting the membrane embedded FO domain with the soluble F1 domain, and the central rotating and curved stalk composed of subunit γε. Although each of the three catalytic binding sites in (αβ)3 catalyzes the same set of partial reactions in the time average, they might not be fully equivalent at any moment, because the structural symmetry is broken by contact with b2δ in F1 and with b2a in FO. We monitored the enzyme’s rotary progression during ATP hydrolysis by three single-molecule techniques: fluorescence video-microscopy with attached actin filaments, Förster resonance energy transfer between pairs of fluorescence probes, and a polarization assay using gold nanorods. We found that one dwell in the three-stepped rotary progression lasting longer than the other two by a factor of up to 1.6. This effect of the structural asymmetry is small due to the internal elastic coupling. View Full-Text
Keywords: FOF1 ATP synthase; Escherichia coli; single-molecule fluorescence; symmetry; cryo-EM structure; subunit rotation; elasticity FOF1 ATP synthase; Escherichia coli; single-molecule fluorescence; symmetry; cryo-EM structure; subunit rotation; elasticity
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Sielaff, H.; Yanagisawa, S.; Frasch, W.D.; Junge, W.; Börsch, M. Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases. Molecules 2019, 24, 504.

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