Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile
Abstract The bacterial enzymes FtsW and FtsI, encoded in the highly conserved dcw gene cluster, are considered to be universally essential for the synthesis of septal peptidoglycan (PG) during cell division. Here, we show that the pathogen Clostridioides difficile lacks a canonical FtsW/FtsI pair, a...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2023-12-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-023-43595-3 |
| _version_ | 1797414707485736960 |
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| author | Shailab Shrestha Najwa Taib Simonetta Gribaldo Aimee Shen |
| author_facet | Shailab Shrestha Najwa Taib Simonetta Gribaldo Aimee Shen |
| author_sort | Shailab Shrestha |
| collection | DOAJ |
| description | Abstract The bacterial enzymes FtsW and FtsI, encoded in the highly conserved dcw gene cluster, are considered to be universally essential for the synthesis of septal peptidoglycan (PG) during cell division. Here, we show that the pathogen Clostridioides difficile lacks a canonical FtsW/FtsI pair, and its dcw-encoded PG synthases have undergone a specialization to fulfill sporulation-specific roles, including synthesizing septal PG during the sporulation-specific mode of cell division. Although these enzymes are directly regulated by canonical divisome components during this process, dcw-encoded PG synthases and their divisome regulators are dispensable for cell division during normal growth. Instead, C. difficile uses a bifunctional class A penicillin-binding protein as the core divisome PG synthase, revealing a previously unreported role for this class of enzymes. Our findings support that the emergence of endosporulation in the Firmicutes phylum facilitated the functional repurposing of cell division factors. Moreover, they indicate that C. difficile, and likely other clostridia, assemble a distinct divisome that therefore may represent a unique target for therapeutic interventions. |
| first_indexed | 2024-03-09T05:37:28Z |
| format | Article |
| id | doaj.art-25e11cb1391945d0bb86708e5cde5dcb |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-03-09T05:37:28Z |
| publishDate | 2023-12-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-25e11cb1391945d0bb86708e5cde5dcb2023-12-03T12:27:37ZengNature PortfolioNature Communications2041-17232023-12-0114111410.1038/s41467-023-43595-3Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficileShailab Shrestha0Najwa Taib1Simonetta Gribaldo2Aimee Shen3Department of Molecular Biology and Microbiology, Tufts University School of MedicineInstitut Pasteur, Université Paris Cité, Evolutionary Biology of the Microbial Cell UnitInstitut Pasteur, Université Paris Cité, Evolutionary Biology of the Microbial Cell UnitDepartment of Molecular Biology and Microbiology, Tufts University School of MedicineAbstract The bacterial enzymes FtsW and FtsI, encoded in the highly conserved dcw gene cluster, are considered to be universally essential for the synthesis of septal peptidoglycan (PG) during cell division. Here, we show that the pathogen Clostridioides difficile lacks a canonical FtsW/FtsI pair, and its dcw-encoded PG synthases have undergone a specialization to fulfill sporulation-specific roles, including synthesizing septal PG during the sporulation-specific mode of cell division. Although these enzymes are directly regulated by canonical divisome components during this process, dcw-encoded PG synthases and their divisome regulators are dispensable for cell division during normal growth. Instead, C. difficile uses a bifunctional class A penicillin-binding protein as the core divisome PG synthase, revealing a previously unreported role for this class of enzymes. Our findings support that the emergence of endosporulation in the Firmicutes phylum facilitated the functional repurposing of cell division factors. Moreover, they indicate that C. difficile, and likely other clostridia, assemble a distinct divisome that therefore may represent a unique target for therapeutic interventions.https://doi.org/10.1038/s41467-023-43595-3 |
| spellingShingle | Shailab Shrestha Najwa Taib Simonetta Gribaldo Aimee Shen Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile Nature Communications |
| title | Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile |
| title_full | Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile |
| title_fullStr | Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile |
| title_full_unstemmed | Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile |
| title_short | Diversification of division mechanisms in endospore-forming bacteria revealed by analyses of peptidoglycan synthesis in Clostridioides difficile |
| title_sort | diversification of division mechanisms in endospore forming bacteria revealed by analyses of peptidoglycan synthesis in clostridioides difficile |
| url | https://doi.org/10.1038/s41467-023-43595-3 |
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