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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...

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Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2023
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.
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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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