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Alternative Architecture of the E. coli Chemosensory Array

Chemotactic responses in motile bacteria are the result of sophisticated signal transduction by large, highly organized arrays of sensory proteins. Despite tremendous progress in the understanding of chemosensory array structure and function, a structural basis for the heightened sensitivity of netw...

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Detalles Bibliográficos
Autores principales: Burt, Alister, Cassidy, C. Keith, Stansfeld, Phillip J., Gutsche, Irina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8064477/
https://www.ncbi.nlm.nih.gov/pubmed/33806045
http://dx.doi.org/10.3390/biom11040495
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author Burt, Alister
Cassidy, C. Keith
Stansfeld, Phillip J.
Gutsche, Irina
author_facet Burt, Alister
Cassidy, C. Keith
Stansfeld, Phillip J.
Gutsche, Irina
author_sort Burt, Alister
collection PubMed
description Chemotactic responses in motile bacteria are the result of sophisticated signal transduction by large, highly organized arrays of sensory proteins. Despite tremendous progress in the understanding of chemosensory array structure and function, a structural basis for the heightened sensitivity of networked chemoreceptors is not yet complete. Here, we present cryo-electron tomography visualisations of native-state chemosensory arrays in E. coli minicells. Strikingly, these arrays appear to exhibit a p2-symmetric array architecture that differs markedly from the p6-symmetric architecture previously described in E. coli. Based on this data, we propose molecular models of this alternative architecture and the canonical p6-symmetric assembly. We evaluate our observations and each model in the context of previously published data, assessing the functional implications of an alternative architecture and effects for future studies.
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spelling pubmed-80644772021-04-24 Alternative Architecture of the E. coli Chemosensory Array Burt, Alister Cassidy, C. Keith Stansfeld, Phillip J. Gutsche, Irina Biomolecules Article Chemotactic responses in motile bacteria are the result of sophisticated signal transduction by large, highly organized arrays of sensory proteins. Despite tremendous progress in the understanding of chemosensory array structure and function, a structural basis for the heightened sensitivity of networked chemoreceptors is not yet complete. Here, we present cryo-electron tomography visualisations of native-state chemosensory arrays in E. coli minicells. Strikingly, these arrays appear to exhibit a p2-symmetric array architecture that differs markedly from the p6-symmetric architecture previously described in E. coli. Based on this data, we propose molecular models of this alternative architecture and the canonical p6-symmetric assembly. We evaluate our observations and each model in the context of previously published data, assessing the functional implications of an alternative architecture and effects for future studies. MDPI 2021-03-25 /pmc/articles/PMC8064477/ /pubmed/33806045 http://dx.doi.org/10.3390/biom11040495 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) ).
spellingShingle Article
Burt, Alister
Cassidy, C. Keith
Stansfeld, Phillip J.
Gutsche, Irina
Alternative Architecture of the E. coli Chemosensory Array
title Alternative Architecture of the E. coli Chemosensory Array
title_full Alternative Architecture of the E. coli Chemosensory Array
title_fullStr Alternative Architecture of the E. coli Chemosensory Array
title_full_unstemmed Alternative Architecture of the E. coli Chemosensory Array
title_short Alternative Architecture of the E. coli Chemosensory Array
title_sort alternative architecture of the e. coli chemosensory array
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8064477/
https://www.ncbi.nlm.nih.gov/pubmed/33806045
http://dx.doi.org/10.3390/biom11040495
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