Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase

Hendrik Sielaff; Dhirendra Singh; Gerhard Grüber; Michael Börsch

doi:10.1117/12.2286785

Analyzing conformational changes in single FRET-labeled A₁ parts of archaeal A₁A_O-ATP synthase

Hendrik Sielaff, Dhirendra Singh, Gerhard Grüber, Michael Börsch

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

1 Citation (Scopus)

Abstract

ATP synthases utilize a proton motive force to synthesize ATP. In reverse, these membrane-embedded enzymes can also hydrolyze ATP to pump protons over the membrane. To prevent wasteful ATP hydrolysis, distinct control mechanisms exist for ATP synthases in bacteria, archaea, chloroplasts and mitochondria. Single-molecule Förster resonance energy transfer (smFRET) demonstrated that the C-terminus of the rotary subunit in the Escherichia coli enzyme changes its conformation to block ATP hydrolysis. Previously, we investigate the related conformational changes of subunit F of the A₁A_O-ATP synthase from the archaeon Methanosarcina mazei Gö1. Here, we analyzed the lifetimes of fluorescence donor and acceptor dyes to distinguish between smFRET signals of conformational changes and potential artefacts.

Original language	English
Title of host publication	Single Molecule Spectroscopy and Superresolution Imaging XI
Editors	Felix Koberling, Ingo Gregor, Jorg Enderlein, Rainer Erdmann, Zygmunt Karol Gryczynski
Publisher	SPIE
ISBN (Electronic)	9781510614857
DOIs	https://doi.org/10.1117/12.2286785
Publication status	Published - 2018
Externally published	Yes
Event	Single Molecule Spectroscopy and Superresolution Imaging XI 2018 - San Francisco, United States Duration: Jan 27 2018 → Jan 28 2018

Publication series

Name	Progress in Biomedical Optics and Imaging - Proceedings of SPIE
Volume	10500
ISSN (Print)	1605-7422

Conference

Conference	Single Molecule Spectroscopy and Superresolution Imaging XI 2018
Country/Territory	United States
City	San Francisco
Period	1/27/18 → 1/28/18

Bibliographical note

Publisher Copyright:
© COPYRIGHT SPIE. Downloading of the abstract is permitted for personal use only.

ASJC Scopus Subject Areas

Electronic, Optical and Magnetic Materials
Biomaterials
Atomic and Molecular Physics, and Optics
Radiology Nuclear Medicine and imaging

Keywords

A1AO-ATP synthase
conformational change
FRET
Methanosarcina mazei Gö1
single molecule

Access to Document

10.1117/12.2286785

Cite this

Sielaff, H., Singh, D., Grüber, G., & Börsch, M. (2018). Analyzing conformational changes in single FRET-labeled A₁ parts of archaeal A₁A_O-ATP synthase. In F. Koberling, I. Gregor, J. Enderlein, R. Erdmann, & Z. K. Gryczynski (Eds.), Single Molecule Spectroscopy and Superresolution Imaging XI Article 1050007 (Progress in Biomedical Optics and Imaging - Proceedings of SPIE; Vol. 10500). SPIE. https://doi.org/10.1117/12.2286785

Sielaff, Hendrik ; Singh, Dhirendra ; Grüber, Gerhard et al. / Analyzing conformational changes in single FRET-labeled A₁ parts of archaeal A₁A_O-ATP synthase. Single Molecule Spectroscopy and Superresolution Imaging XI. editor / Felix Koberling ; Ingo Gregor ; Jorg Enderlein ; Rainer Erdmann ; Zygmunt Karol Gryczynski. SPIE, 2018. (Progress in Biomedical Optics and Imaging - Proceedings of SPIE).

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abstract = "ATP synthases utilize a proton motive force to synthesize ATP. In reverse, these membrane-embedded enzymes can also hydrolyze ATP to pump protons over the membrane. To prevent wasteful ATP hydrolysis, distinct control mechanisms exist for ATP synthases in bacteria, archaea, chloroplasts and mitochondria. Single-molecule F{\"o}rster resonance energy transfer (smFRET) demonstrated that the C-terminus of the rotary subunit in the Escherichia coli enzyme changes its conformation to block ATP hydrolysis. Previously, we investigate the related conformational changes of subunit F of the A1AO-ATP synthase from the archaeon Methanosarcina mazei G{\"o}1. Here, we analyzed the lifetimes of fluorescence donor and acceptor dyes to distinguish between smFRET signals of conformational changes and potential artefacts.",

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Sielaff, H, Singh, D, Grüber, G & Börsch, M 2018, Analyzing conformational changes in single FRET-labeled A₁ parts of archaeal A₁A_O-ATP synthase. in F Koberling, I Gregor, J Enderlein, R Erdmann & ZK Gryczynski (eds), Single Molecule Spectroscopy and Superresolution Imaging XI., 1050007, Progress in Biomedical Optics and Imaging - Proceedings of SPIE, vol. 10500, SPIE, Single Molecule Spectroscopy and Superresolution Imaging XI 2018, San Francisco, United States, 1/27/18. https://doi.org/10.1117/12.2286785

Analyzing conformational changes in single FRET-labeled A₁ parts of archaeal A₁A_O-ATP synthase. / Sielaff, Hendrik; Singh, Dhirendra; Grüber, Gerhard et al.
Single Molecule Spectroscopy and Superresolution Imaging XI. ed. / Felix Koberling; Ingo Gregor; Jorg Enderlein; Rainer Erdmann; Zygmunt Karol Gryczynski. SPIE, 2018. 1050007 (Progress in Biomedical Optics and Imaging - Proceedings of SPIE; Vol. 10500).

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

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AU - Börsch, Michael

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N2 - ATP synthases utilize a proton motive force to synthesize ATP. In reverse, these membrane-embedded enzymes can also hydrolyze ATP to pump protons over the membrane. To prevent wasteful ATP hydrolysis, distinct control mechanisms exist for ATP synthases in bacteria, archaea, chloroplasts and mitochondria. Single-molecule Förster resonance energy transfer (smFRET) demonstrated that the C-terminus of the rotary subunit in the Escherichia coli enzyme changes its conformation to block ATP hydrolysis. Previously, we investigate the related conformational changes of subunit F of the A1AO-ATP synthase from the archaeon Methanosarcina mazei Gö1. Here, we analyzed the lifetimes of fluorescence donor and acceptor dyes to distinguish between smFRET signals of conformational changes and potential artefacts.

AB - ATP synthases utilize a proton motive force to synthesize ATP. In reverse, these membrane-embedded enzymes can also hydrolyze ATP to pump protons over the membrane. To prevent wasteful ATP hydrolysis, distinct control mechanisms exist for ATP synthases in bacteria, archaea, chloroplasts and mitochondria. Single-molecule Förster resonance energy transfer (smFRET) demonstrated that the C-terminus of the rotary subunit in the Escherichia coli enzyme changes its conformation to block ATP hydrolysis. Previously, we investigate the related conformational changes of subunit F of the A1AO-ATP synthase from the archaeon Methanosarcina mazei Gö1. Here, we analyzed the lifetimes of fluorescence donor and acceptor dyes to distinguish between smFRET signals of conformational changes and potential artefacts.

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Sielaff H, Singh D, Grüber G, Börsch M. Analyzing conformational changes in single FRET-labeled A₁ parts of archaeal A₁A_O-ATP synthase. In Koberling F, Gregor I, Enderlein J, Erdmann R, Gryczynski ZK, editors, Single Molecule Spectroscopy and Superresolution Imaging XI. SPIE. 2018. 1050007. (Progress in Biomedical Optics and Imaging - Proceedings of SPIE). doi: 10.1117/12.2286785