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Molecular basis of the final step of cell division in Streptococcus pneumoniae
Bacterial cell-wall hydrolases must be tightly regulated during bacterial cell division to prevent aberrant cell lysis and to allow final separation of viable daughter cells. In a multidisciplinary work, we disclose the molecular dialogue between the cell-wall hydrolase LytB, wall teichoic acids, an...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10434722/ https://www.ncbi.nlm.nih.gov/pubmed/37418323 http://dx.doi.org/10.1016/j.celrep.2023.112756 |
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author | Martínez-Caballero, Siseth Freton, Céline Molina, Rafael Bartual, Sergio G. Gueguen-Chaignon, Virginie Mercy, Chryslène Gago, Federico Mahasenan, Kiran V. Muñoz, Inés G. Lee, Mijoon Hesek, Dusan Mobashery, Shahriar Hermoso, Juan A. Grangeasse, Christophe |
author_facet | Martínez-Caballero, Siseth Freton, Céline Molina, Rafael Bartual, Sergio G. Gueguen-Chaignon, Virginie Mercy, Chryslène Gago, Federico Mahasenan, Kiran V. Muñoz, Inés G. Lee, Mijoon Hesek, Dusan Mobashery, Shahriar Hermoso, Juan A. Grangeasse, Christophe |
author_sort | Martínez-Caballero, Siseth |
collection | PubMed |
description | Bacterial cell-wall hydrolases must be tightly regulated during bacterial cell division to prevent aberrant cell lysis and to allow final separation of viable daughter cells. In a multidisciplinary work, we disclose the molecular dialogue between the cell-wall hydrolase LytB, wall teichoic acids, and the eukaryotic-like protein kinase StkP in Streptococcus pneumoniae. After characterizing the peptidoglycan recognition mode by the catalytic domain of LytB, we further demonstrate that LytB possesses a modular organization allowing the specific binding to wall teichoic acids and to the protein kinase StkP. Structural and cellular studies notably reveal that the temporal and spatial localization of LytB is governed by the interaction between specific modules of LytB and the final PASTA domain of StkP. Our data collectively provide a comprehensive understanding of how LytB performs final separation of daughter cells and highlights the regulatory role of eukaryotic-like kinases on lytic machineries in the last step of cell division in streptococci. |
format | Online Article Text |
id | pubmed-10434722 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
record_format | MEDLINE/PubMed |
spelling | pubmed-104347222023-08-17 Molecular basis of the final step of cell division in Streptococcus pneumoniae Martínez-Caballero, Siseth Freton, Céline Molina, Rafael Bartual, Sergio G. Gueguen-Chaignon, Virginie Mercy, Chryslène Gago, Federico Mahasenan, Kiran V. Muñoz, Inés G. Lee, Mijoon Hesek, Dusan Mobashery, Shahriar Hermoso, Juan A. Grangeasse, Christophe Cell Rep Article Bacterial cell-wall hydrolases must be tightly regulated during bacterial cell division to prevent aberrant cell lysis and to allow final separation of viable daughter cells. In a multidisciplinary work, we disclose the molecular dialogue between the cell-wall hydrolase LytB, wall teichoic acids, and the eukaryotic-like protein kinase StkP in Streptococcus pneumoniae. After characterizing the peptidoglycan recognition mode by the catalytic domain of LytB, we further demonstrate that LytB possesses a modular organization allowing the specific binding to wall teichoic acids and to the protein kinase StkP. Structural and cellular studies notably reveal that the temporal and spatial localization of LytB is governed by the interaction between specific modules of LytB and the final PASTA domain of StkP. Our data collectively provide a comprehensive understanding of how LytB performs final separation of daughter cells and highlights the regulatory role of eukaryotic-like kinases on lytic machineries in the last step of cell division in streptococci. 2023-07-25 2023-07-06 /pmc/articles/PMC10434722/ /pubmed/37418323 http://dx.doi.org/10.1016/j.celrep.2023.112756 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) ). |
spellingShingle | Article Martínez-Caballero, Siseth Freton, Céline Molina, Rafael Bartual, Sergio G. Gueguen-Chaignon, Virginie Mercy, Chryslène Gago, Federico Mahasenan, Kiran V. Muñoz, Inés G. Lee, Mijoon Hesek, Dusan Mobashery, Shahriar Hermoso, Juan A. Grangeasse, Christophe Molecular basis of the final step of cell division in Streptococcus pneumoniae |
title | Molecular basis of the final step of cell division in Streptococcus pneumoniae |
title_full | Molecular basis of the final step of cell division in Streptococcus pneumoniae |
title_fullStr | Molecular basis of the final step of cell division in Streptococcus pneumoniae |
title_full_unstemmed | Molecular basis of the final step of cell division in Streptococcus pneumoniae |
title_short | Molecular basis of the final step of cell division in Streptococcus pneumoniae |
title_sort | molecular basis of the final step of cell division in streptococcus pneumoniae |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10434722/ https://www.ncbi.nlm.nih.gov/pubmed/37418323 http://dx.doi.org/10.1016/j.celrep.2023.112756 |
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