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The Staphylococcus aureus cell division protein, DivIC, interacts with the cell wall and controls its biosynthesis

Bacterial cell division is a complex, dynamic process that requires multiple protein components to orchestrate its progression. Many division proteins are highly conserved across bacterial species alluding to a common, basic mechanism. Central to division is a transmembrane trimeric complex involvin...

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Autores principales: Tinajero-Trejo, Mariana, Carnell, Oliver, Kabli, Azhar F., Pasquina-Lemonche, Laia, Lafage, Lucia, Han, Aidong, Hobbs, Jamie K., Foster, Simon J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9652317/
https://www.ncbi.nlm.nih.gov/pubmed/36369270
http://dx.doi.org/10.1038/s42003-022-04161-7
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author Tinajero-Trejo, Mariana
Carnell, Oliver
Kabli, Azhar F.
Pasquina-Lemonche, Laia
Lafage, Lucia
Han, Aidong
Hobbs, Jamie K.
Foster, Simon J.
author_facet Tinajero-Trejo, Mariana
Carnell, Oliver
Kabli, Azhar F.
Pasquina-Lemonche, Laia
Lafage, Lucia
Han, Aidong
Hobbs, Jamie K.
Foster, Simon J.
author_sort Tinajero-Trejo, Mariana
collection PubMed
description Bacterial cell division is a complex, dynamic process that requires multiple protein components to orchestrate its progression. Many division proteins are highly conserved across bacterial species alluding to a common, basic mechanism. Central to division is a transmembrane trimeric complex involving DivIB, DivIC and FtsL in Gram-positives. Here, we show a distinct, essential role for DivIC in division and survival of Staphylococcus aureus. DivIC spatially regulates peptidoglycan synthesis, and consequently cell wall architecture, by influencing the recruitment to the division septum of the major peptidoglycan synthetases PBP2 and FtsW. Both the function of DivIC and its recruitment to the division site depend on its extracellular domain, which interacts with the cell wall via binding to wall teichoic acids. DivIC facilitates the spatial and temporal coordination of peptidoglycan synthesis with the developing architecture of the septum during cell division. A better understanding of the cell division mechanisms in S. aureus and other pathogenic microorganisms can provide possibilities for the development of new, more effective treatments for bacterial infections.
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spelling pubmed-96523172022-11-15 The Staphylococcus aureus cell division protein, DivIC, interacts with the cell wall and controls its biosynthesis Tinajero-Trejo, Mariana Carnell, Oliver Kabli, Azhar F. Pasquina-Lemonche, Laia Lafage, Lucia Han, Aidong Hobbs, Jamie K. Foster, Simon J. Commun Biol Article Bacterial cell division is a complex, dynamic process that requires multiple protein components to orchestrate its progression. Many division proteins are highly conserved across bacterial species alluding to a common, basic mechanism. Central to division is a transmembrane trimeric complex involving DivIB, DivIC and FtsL in Gram-positives. Here, we show a distinct, essential role for DivIC in division and survival of Staphylococcus aureus. DivIC spatially regulates peptidoglycan synthesis, and consequently cell wall architecture, by influencing the recruitment to the division septum of the major peptidoglycan synthetases PBP2 and FtsW. Both the function of DivIC and its recruitment to the division site depend on its extracellular domain, which interacts with the cell wall via binding to wall teichoic acids. DivIC facilitates the spatial and temporal coordination of peptidoglycan synthesis with the developing architecture of the septum during cell division. A better understanding of the cell division mechanisms in S. aureus and other pathogenic microorganisms can provide possibilities for the development of new, more effective treatments for bacterial infections. Nature Publishing Group UK 2022-11-11 /pmc/articles/PMC9652317/ /pubmed/36369270 http://dx.doi.org/10.1038/s42003-022-04161-7 Text en © The Author(s) 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
Tinajero-Trejo, Mariana
Carnell, Oliver
Kabli, Azhar F.
Pasquina-Lemonche, Laia
Lafage, Lucia
Han, Aidong
Hobbs, Jamie K.
Foster, Simon J.
The Staphylococcus aureus cell division protein, DivIC, interacts with the cell wall and controls its biosynthesis
title The Staphylococcus aureus cell division protein, DivIC, interacts with the cell wall and controls its biosynthesis
title_full The Staphylococcus aureus cell division protein, DivIC, interacts with the cell wall and controls its biosynthesis
title_fullStr The Staphylococcus aureus cell division protein, DivIC, interacts with the cell wall and controls its biosynthesis
title_full_unstemmed The Staphylococcus aureus cell division protein, DivIC, interacts with the cell wall and controls its biosynthesis
title_short The Staphylococcus aureus cell division protein, DivIC, interacts with the cell wall and controls its biosynthesis
title_sort staphylococcus aureus cell division protein, divic, interacts with the cell wall and controls its biosynthesis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9652317/
https://www.ncbi.nlm.nih.gov/pubmed/36369270
http://dx.doi.org/10.1038/s42003-022-04161-7
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