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Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain
Motile bacteria sense chemical gradients with transmembrane receptors organised in supramolecular signalling arrays. Understanding stimulus detection and transmission at the molecular level requires precise structural characterisation of the array building block known as a core signalling unit. Here...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7005262/ https://www.ncbi.nlm.nih.gov/pubmed/32029744 http://dx.doi.org/10.1038/s41467-020-14350-9 |
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author | Burt, Alister Cassidy, C. Keith Ames, Peter Bacia-Verloop, Maria Baulard, Megghane Huard, Karine Luthey-Schulten, Zaida Desfosses, Ambroise Stansfeld, Phillip J. Margolin, William Parkinson, John S. Gutsche, Irina |
author_facet | Burt, Alister Cassidy, C. Keith Ames, Peter Bacia-Verloop, Maria Baulard, Megghane Huard, Karine Luthey-Schulten, Zaida Desfosses, Ambroise Stansfeld, Phillip J. Margolin, William Parkinson, John S. Gutsche, Irina |
author_sort | Burt, Alister |
collection | PubMed |
description | Motile bacteria sense chemical gradients with transmembrane receptors organised in supramolecular signalling arrays. Understanding stimulus detection and transmission at the molecular level requires precise structural characterisation of the array building block known as a core signalling unit. Here we introduce an Escherichia coli strain that forms small minicells possessing extended and highly ordered chemosensory arrays. We use cryo-electron tomography and subtomogram averaging to provide a three-dimensional map of a complete core signalling unit, with visible densities corresponding to the HAMP and periplasmic domains. This map, combined with previously determined high resolution structures and molecular dynamics simulations, yields a molecular model of the transmembrane core signalling unit and enables spatial localisation of its individual domains. Our work thus offers a solid structural basis for the interpretation of a wide range of existing data and the design of further experiments to elucidate signalling mechanisms within the core signalling unit and larger array. |
format | Online Article Text |
id | pubmed-7005262 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-70052622020-02-10 Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain Burt, Alister Cassidy, C. Keith Ames, Peter Bacia-Verloop, Maria Baulard, Megghane Huard, Karine Luthey-Schulten, Zaida Desfosses, Ambroise Stansfeld, Phillip J. Margolin, William Parkinson, John S. Gutsche, Irina Nat Commun Article Motile bacteria sense chemical gradients with transmembrane receptors organised in supramolecular signalling arrays. Understanding stimulus detection and transmission at the molecular level requires precise structural characterisation of the array building block known as a core signalling unit. Here we introduce an Escherichia coli strain that forms small minicells possessing extended and highly ordered chemosensory arrays. We use cryo-electron tomography and subtomogram averaging to provide a three-dimensional map of a complete core signalling unit, with visible densities corresponding to the HAMP and periplasmic domains. This map, combined with previously determined high resolution structures and molecular dynamics simulations, yields a molecular model of the transmembrane core signalling unit and enables spatial localisation of its individual domains. Our work thus offers a solid structural basis for the interpretation of a wide range of existing data and the design of further experiments to elucidate signalling mechanisms within the core signalling unit and larger array. Nature Publishing Group UK 2020-02-06 /pmc/articles/PMC7005262/ /pubmed/32029744 http://dx.doi.org/10.1038/s41467-020-14350-9 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Burt, Alister Cassidy, C. Keith Ames, Peter Bacia-Verloop, Maria Baulard, Megghane Huard, Karine Luthey-Schulten, Zaida Desfosses, Ambroise Stansfeld, Phillip J. Margolin, William Parkinson, John S. Gutsche, Irina Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain |
title | Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain |
title_full | Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain |
title_fullStr | Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain |
title_full_unstemmed | Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain |
title_short | Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain |
title_sort | complete structure of the chemosensory array core signalling unit in an e. coli minicell strain |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7005262/ https://www.ncbi.nlm.nih.gov/pubmed/32029744 http://dx.doi.org/10.1038/s41467-020-14350-9 |
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