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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
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.
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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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