Self-association of MreC as a regulatory signal in bacterial cell wall elongation
MreC is a membrane-associated protein that modulates the activity of the elongasome, a protein complex that controls cell wall formation in rod-shaped bacteria. Here, the authors use electron cryo-microscopy and X-ray crystallography to determine the structure of a self-associated form of MreC in at...
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2021-05-01
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doaj-bfd9056a555a4b14acc5e2a6e24d19b12021-05-23T11:13:55ZengNature Publishing GroupNature Communications2041-17232021-05-0112111010.1038/s41467-021-22957-9Self-association of MreC as a regulatory signal in bacterial cell wall elongationAlexandre Martins0Carlos Contreras-Martel1Manon Janet-Maitre2Mayara M. Miyachiro3Leandro F. Estrozi4Daniel Maragno Trindade5Caíque C. Malospirito6Fernanda Rodrigues-Costa7Lionel Imbert8Viviana Job9Guy Schoehn10Ina Attrée11Andréa Dessen12Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)Brazilian Biosciences National Laboratory (LNBio), CNPEMBrazilian Biosciences National Laboratory (LNBio), CNPEMBrazilian Biosciences National Laboratory (LNBio), CNPEMUniv. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS)MreC is a membrane-associated protein that modulates the activity of the elongasome, a protein complex that controls cell wall formation in rod-shaped bacteria. Here, the authors use electron cryo-microscopy and X-ray crystallography to determine the structure of a self-associated form of MreC in atomic detail.https://doi.org/10.1038/s41467-021-22957-9 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Alexandre Martins Carlos Contreras-Martel Manon Janet-Maitre Mayara M. Miyachiro Leandro F. Estrozi Daniel Maragno Trindade Caíque C. Malospirito Fernanda Rodrigues-Costa Lionel Imbert Viviana Job Guy Schoehn Ina Attrée Andréa Dessen |
spellingShingle |
Alexandre Martins Carlos Contreras-Martel Manon Janet-Maitre Mayara M. Miyachiro Leandro F. Estrozi Daniel Maragno Trindade Caíque C. Malospirito Fernanda Rodrigues-Costa Lionel Imbert Viviana Job Guy Schoehn Ina Attrée Andréa Dessen Self-association of MreC as a regulatory signal in bacterial cell wall elongation Nature Communications |
author_facet |
Alexandre Martins Carlos Contreras-Martel Manon Janet-Maitre Mayara M. Miyachiro Leandro F. Estrozi Daniel Maragno Trindade Caíque C. Malospirito Fernanda Rodrigues-Costa Lionel Imbert Viviana Job Guy Schoehn Ina Attrée Andréa Dessen |
author_sort |
Alexandre Martins |
title |
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_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_sort |
self-association of mrec as a regulatory signal in bacterial cell wall elongation |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2021-05-01 |
description |
MreC is a membrane-associated protein that modulates the activity of the elongasome, a protein complex that controls cell wall formation in rod-shaped bacteria. Here, the authors use electron cryo-microscopy and X-ray crystallography to determine the structure of a self-associated form of MreC in atomic detail. |
url |
https://doi.org/10.1038/s41467-021-22957-9 |
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