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

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

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 mitochon...

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Main Authors: Sielaff, Hendrik, Singh, Dhirendra, Grüber, Gerhard, Börsch, Michael
Other Authors: Enderlein, Jörg
Format: Article
Language:English
Published: 2018
Subjects:
Conformational Change
A1AO-ATP Synthase
DRNTU::Science::Biological sciences
Online Access:https://hdl.handle.net/10356/88875
http://hdl.handle.net/10220/45931
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-888752023-02-28T16:58:37Z Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase Sielaff, Hendrik Singh, Dhirendra Grüber, Gerhard Börsch, Michael Enderlein, Jörg Gregor, Ingo Gryczynski, Zygmunt K. Erdmann, Rainer Koberling, Felix School of Biological Sciences Single Molecule Spectroscopy and Superresolution Imaging XI Conformational Change A1AO-ATP Synthase DRNTU::Science::Biological sciences 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 ε 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. MOE (Min. of Education, S’pore) NMRC (Natl Medical Research Council, S’pore) Published version 2018-09-11T04:06:02Z 2019-12-06T17:12:53Z 2018-09-11T04:06:02Z 2019-12-06T17:12:53Z 2018 Journal Article Sielaff, H., Singh, D., Grüber, G., & Börsch, M. (2018). Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase. Progress in Biomedical Optics and Imaging - Proceedings of SPIE, 10500, 1050007-. doi:10.1117/12.2286785 https://hdl.handle.net/10356/88875 http://hdl.handle.net/10220/45931 10.1117/12.2286785 en Progress in Biomedical Optics and Imaging - Proceedings of SPIE © 2018 Society of Photo-optical Instrumentation Engineers (SPIE). This paper was published in Progress in Biomedical Optics and Imaging - Proceedings of SPIE and is made available with permission of Society of Photo-optical Instrumentation Engineers (SPIE). The published version is available at: [http://dx.doi.org/10.1117/12.2286785]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law. 12 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Conformational Change
A1AO-ATP Synthase
DRNTU::Science::Biological sciences
spellingShingle Conformational Change
A1AO-ATP Synthase
DRNTU::Science::Biological sciences
Sielaff, Hendrik
Singh, Dhirendra
Grüber, Gerhard
Börsch, Michael
Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase
description 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 ε 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.
author2 Enderlein, Jörg
author_facet Enderlein, Jörg
Sielaff, Hendrik
Singh, Dhirendra
Grüber, Gerhard
Börsch, Michael
format Article
author Sielaff, Hendrik
Singh, Dhirendra
Grüber, Gerhard
Börsch, Michael
author_sort Sielaff, Hendrik
title Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase
title_short Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase
title_full Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase
title_fullStr Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase
title_full_unstemmed Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase
title_sort analyzing conformational changes in single fret-labeled a1 parts of archaeal a1ao-atp synthase
publishDate 2018
url https://hdl.handle.net/10356/88875
http://hdl.handle.net/10220/45931
_version_ 1759857585599545344

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