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Self-association of MreC as a regulatory signal in bacterial cell wall elongation
The elongasome, or Rod system, is a protein complex that controls cell wall formation in rod-shaped bacteria. MreC is a membrane-associated elongasome component that co-localizes with the cytoskeletal element MreB and regulates the activity of cell wall biosynthesis enzymes, in a process that may be...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8137920/ https://www.ncbi.nlm.nih.gov/pubmed/34016967 http://dx.doi.org/10.1038/s41467-021-22957-9 |
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author | Martins, Alexandre Contreras-Martel, Carlos Janet-Maitre, Manon Miyachiro, Mayara M. Estrozi, Leandro F. Trindade, Daniel Maragno Malospirito, Caíque C. Rodrigues-Costa, Fernanda Imbert, Lionel Job, Viviana Schoehn, Guy Attrée, Ina Dessen, Andréa |
author_facet | Martins, Alexandre Contreras-Martel, Carlos Janet-Maitre, Manon Miyachiro, Mayara M. Estrozi, Leandro F. Trindade, Daniel Maragno Malospirito, Caíque C. Rodrigues-Costa, Fernanda Imbert, Lionel Job, Viviana Schoehn, Guy Attrée, Ina Dessen, Andréa |
author_sort | Martins, Alexandre |
collection | PubMed |
description | The elongasome, or Rod system, is a protein complex that controls cell wall formation in rod-shaped bacteria. MreC is a membrane-associated elongasome component that co-localizes with the cytoskeletal element MreB and regulates the activity of cell wall biosynthesis enzymes, in a process that may be dependent on MreC self-association. Here, we use electron cryo-microscopy and X-ray crystallography to determine the structure of a self-associated form of MreC from Pseudomonas aeruginosa in atomic detail. MreC monomers interact in head-to-tail fashion. Longitudinal and lateral interfaces are essential for oligomerization in vitro, and a phylogenetic analysis of proteobacterial MreC sequences indicates the prevalence of the identified interfaces. Our results are consistent with a model where MreC’s ability to alternate between self-association and interaction with the cell wall biosynthesis machinery plays a key role in the regulation of elongasome activity. |
format | Online Article Text |
id | pubmed-8137920 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-81379202021-06-03 Self-association of MreC as a regulatory signal in bacterial cell wall elongation Martins, Alexandre Contreras-Martel, Carlos Janet-Maitre, Manon Miyachiro, Mayara M. Estrozi, Leandro F. Trindade, Daniel Maragno Malospirito, Caíque C. Rodrigues-Costa, Fernanda Imbert, Lionel Job, Viviana Schoehn, Guy Attrée, Ina Dessen, Andréa Nat Commun Article The elongasome, or Rod system, is a protein complex that controls cell wall formation in rod-shaped bacteria. MreC is a membrane-associated elongasome component that co-localizes with the cytoskeletal element MreB and regulates the activity of cell wall biosynthesis enzymes, in a process that may be dependent on MreC self-association. Here, we use electron cryo-microscopy and X-ray crystallography to determine the structure of a self-associated form of MreC from Pseudomonas aeruginosa in atomic detail. MreC monomers interact in head-to-tail fashion. Longitudinal and lateral interfaces are essential for oligomerization in vitro, and a phylogenetic analysis of proteobacterial MreC sequences indicates the prevalence of the identified interfaces. Our results are consistent with a model where MreC’s ability to alternate between self-association and interaction with the cell wall biosynthesis machinery plays a key role in the regulation of elongasome activity. Nature Publishing Group UK 2021-05-20 /pmc/articles/PMC8137920/ /pubmed/34016967 http://dx.doi.org/10.1038/s41467-021-22957-9 Text en © The Author(s) 2021, corrected publication 2022 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Martins, Alexandre Contreras-Martel, Carlos Janet-Maitre, Manon Miyachiro, Mayara M. Estrozi, Leandro F. Trindade, Daniel Maragno Malospirito, Caíque C. Rodrigues-Costa, Fernanda Imbert, Lionel Job, Viviana Schoehn, Guy Attrée, Ina Dessen, Andréa Self-association of MreC as a regulatory signal in bacterial cell wall elongation |
title | Self-association of MreC as a regulatory signal in bacterial cell wall elongation |
title_full | Self-association of MreC as a regulatory signal in bacterial cell wall elongation |
title_fullStr | Self-association of MreC as a regulatory signal in bacterial cell wall elongation |
title_full_unstemmed | Self-association of MreC as a regulatory signal in bacterial cell wall elongation |
title_short | Self-association of MreC as a regulatory signal in bacterial cell wall elongation |
title_sort | self-association of mrec as a regulatory signal in bacterial cell wall elongation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8137920/ https://www.ncbi.nlm.nih.gov/pubmed/34016967 http://dx.doi.org/10.1038/s41467-021-22957-9 |
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