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Both piston-like and rotational motions are present in bacterial chemoreceptor signaling

Bacterial chemotaxis signaling is triggered by binding of chemo-effectors to the membrane-bound chemoreceptor dimers. Though much is known about the structure of the chemoreceptors, details of the receptor dynamics and their effects on signaling are still unclear. Here, by using molecular dynamics s...

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Detalles Bibliográficos
Autores principales: Yu, Daqi, Ma, Xiaomin, Tu, Yuhai, Lai, Luhua
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4345343/
https://www.ncbi.nlm.nih.gov/pubmed/25728261
http://dx.doi.org/10.1038/srep08640
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author Yu, Daqi
Ma, Xiaomin
Tu, Yuhai
Lai, Luhua
author_facet Yu, Daqi
Ma, Xiaomin
Tu, Yuhai
Lai, Luhua
author_sort Yu, Daqi
collection PubMed
description Bacterial chemotaxis signaling is triggered by binding of chemo-effectors to the membrane-bound chemoreceptor dimers. Though much is known about the structure of the chemoreceptors, details of the receptor dynamics and their effects on signaling are still unclear. Here, by using molecular dynamics simulations and principle component analysis, we study the dynamics of the periplasmic domain of aspartate chemoreceptor Tar dimer and its conformational changes when binding to different ligands (attractant, antagonist, and two attractant molecules). We found two dominant components (modes) in the receptor dynamics: a relative rotation of the two Tar monomers and a piston-like up-and-down sliding movement of the α4 helix. These two modes are highly correlated. Binding of one attractant molecule to the Tar dimer induced both significant piston-like downward movements of the α4 helix and strong relative rotations of the two Tar monomers, while binding of an antagonist or the symmetric binding of two attractant molecules to a Tar dimer suppresses both modes. The anti-symmetric effects of the relative rotation mode also explained the negative cooperativity between the two binding pockets. Our results suggest a mechanism of coupled rotation and piston-like motion for bacterial chemoreceptor signaling.
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spelling pubmed-43453432015-03-10 Both piston-like and rotational motions are present in bacterial chemoreceptor signaling Yu, Daqi Ma, Xiaomin Tu, Yuhai Lai, Luhua Sci Rep Article Bacterial chemotaxis signaling is triggered by binding of chemo-effectors to the membrane-bound chemoreceptor dimers. Though much is known about the structure of the chemoreceptors, details of the receptor dynamics and their effects on signaling are still unclear. Here, by using molecular dynamics simulations and principle component analysis, we study the dynamics of the periplasmic domain of aspartate chemoreceptor Tar dimer and its conformational changes when binding to different ligands (attractant, antagonist, and two attractant molecules). We found two dominant components (modes) in the receptor dynamics: a relative rotation of the two Tar monomers and a piston-like up-and-down sliding movement of the α4 helix. These two modes are highly correlated. Binding of one attractant molecule to the Tar dimer induced both significant piston-like downward movements of the α4 helix and strong relative rotations of the two Tar monomers, while binding of an antagonist or the symmetric binding of two attractant molecules to a Tar dimer suppresses both modes. The anti-symmetric effects of the relative rotation mode also explained the negative cooperativity between the two binding pockets. Our results suggest a mechanism of coupled rotation and piston-like motion for bacterial chemoreceptor signaling. Nature Publishing Group 2015-03-02 /pmc/articles/PMC4345343/ /pubmed/25728261 http://dx.doi.org/10.1038/srep08640 Text en Copyright © 2015, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Yu, Daqi
Ma, Xiaomin
Tu, Yuhai
Lai, Luhua
Both piston-like and rotational motions are present in bacterial chemoreceptor signaling
title Both piston-like and rotational motions are present in bacterial chemoreceptor signaling
title_full Both piston-like and rotational motions are present in bacterial chemoreceptor signaling
title_fullStr Both piston-like and rotational motions are present in bacterial chemoreceptor signaling
title_full_unstemmed Both piston-like and rotational motions are present in bacterial chemoreceptor signaling
title_short Both piston-like and rotational motions are present in bacterial chemoreceptor signaling
title_sort both piston-like and rotational motions are present in bacterial chemoreceptor signaling
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4345343/
https://www.ncbi.nlm.nih.gov/pubmed/25728261
http://dx.doi.org/10.1038/srep08640
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