Minimization of the Bacillus subtilis divisome suggests FtsZ and SepF can form an active Z-ring, and reveals the amino acid transporter BraB as a new cell division influencing factor.
Bacterial cytokinesis begins with polymerization of the tubulin homologue FtsZ into a ring-like structure at midcell, the Z-ring, which recruits the late cell division proteins that synthesize the division septum. Assembly of FtsZ is carefully regulated and supported by a dozen conserved cell divisi...
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Public Library of Science (PLoS)
2025-01-01
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| Series: | PLoS Genetics |
| Online Access: | https://doi.org/10.1371/journal.pgen.1011567 |
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| author | Ilkay Celik Gulsoy Terrens N V Saaki Michaela Wenzel Simon Syvertsson Taku Morimoto Tjalling K Siersma Leendert W Hamoen |
| author_facet | Ilkay Celik Gulsoy Terrens N V Saaki Michaela Wenzel Simon Syvertsson Taku Morimoto Tjalling K Siersma Leendert W Hamoen |
| author_sort | Ilkay Celik Gulsoy |
| collection | DOAJ |
| description | Bacterial cytokinesis begins with polymerization of the tubulin homologue FtsZ into a ring-like structure at midcell, the Z-ring, which recruits the late cell division proteins that synthesize the division septum. Assembly of FtsZ is carefully regulated and supported by a dozen conserved cell division proteins. Generally, these proteins are not essential, but removing more than one is in many cases lethal. Therefore, it is still not fully clear how the different protein components contribute to cell division, and whether there is a minimal set of proteins that can execute cell division. In this study, we tried to find the minimal set of proteins that is required to establish an active Z-ring in the model bacterium Bacillus subtilis. By making use of known suppressor mutations we were able to find a gene deletion route that eventually enabled us the remove eight conserved cell division proteins: ZapA, MinC, MinJ, UgtP, ClpX, Noc, EzrA and FtsA. Only FtsZ and its membrane anchor SepF appeared to be required for Z-ring formation. Interestingly, SepF is also the FtsZ anchor in archaea, and both proteins date back to the Last Universal Common Ancestor (LUCA). Viability of the multiple deletion mutant was not greatly affected, although the frequency of cell division was considerably reduced. Whole genome sequencing suggested that the construction of this minimal divisome strain was also possible due to the accumulation of suppressor mutations. After extensive phenotypic testing of these mutations, we found an unexpected cell division regulation function for the branched chain amino acid transporter BraB, which may be related to a change in fatty acid composition. The implications of these findings for the role of SepF, and the construction of a minimal cell division machinery are discussed. |
| format | Article |
| id | doaj-art-916cd1a1424b42f1b69c4d4371c0ce4f |
| institution | Kabale University |
| issn | 1553-7390 1553-7404 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Genetics |
| spelling | doaj-art-916cd1a1424b42f1b69c4d4371c0ce4f2025-02-07T05:30:35ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042025-01-01211e101156710.1371/journal.pgen.1011567Minimization of the Bacillus subtilis divisome suggests FtsZ and SepF can form an active Z-ring, and reveals the amino acid transporter BraB as a new cell division influencing factor.Ilkay Celik GulsoyTerrens N V SaakiMichaela WenzelSimon SyvertssonTaku MorimotoTjalling K SiersmaLeendert W HamoenBacterial cytokinesis begins with polymerization of the tubulin homologue FtsZ into a ring-like structure at midcell, the Z-ring, which recruits the late cell division proteins that synthesize the division septum. Assembly of FtsZ is carefully regulated and supported by a dozen conserved cell division proteins. Generally, these proteins are not essential, but removing more than one is in many cases lethal. Therefore, it is still not fully clear how the different protein components contribute to cell division, and whether there is a minimal set of proteins that can execute cell division. In this study, we tried to find the minimal set of proteins that is required to establish an active Z-ring in the model bacterium Bacillus subtilis. By making use of known suppressor mutations we were able to find a gene deletion route that eventually enabled us the remove eight conserved cell division proteins: ZapA, MinC, MinJ, UgtP, ClpX, Noc, EzrA and FtsA. Only FtsZ and its membrane anchor SepF appeared to be required for Z-ring formation. Interestingly, SepF is also the FtsZ anchor in archaea, and both proteins date back to the Last Universal Common Ancestor (LUCA). Viability of the multiple deletion mutant was not greatly affected, although the frequency of cell division was considerably reduced. Whole genome sequencing suggested that the construction of this minimal divisome strain was also possible due to the accumulation of suppressor mutations. After extensive phenotypic testing of these mutations, we found an unexpected cell division regulation function for the branched chain amino acid transporter BraB, which may be related to a change in fatty acid composition. The implications of these findings for the role of SepF, and the construction of a minimal cell division machinery are discussed.https://doi.org/10.1371/journal.pgen.1011567 |
| spellingShingle | Ilkay Celik Gulsoy Terrens N V Saaki Michaela Wenzel Simon Syvertsson Taku Morimoto Tjalling K Siersma Leendert W Hamoen Minimization of the Bacillus subtilis divisome suggests FtsZ and SepF can form an active Z-ring, and reveals the amino acid transporter BraB as a new cell division influencing factor. PLoS Genetics |
| title | Minimization of the Bacillus subtilis divisome suggests FtsZ and SepF can form an active Z-ring, and reveals the amino acid transporter BraB as a new cell division influencing factor. |
| title_full | Minimization of the Bacillus subtilis divisome suggests FtsZ and SepF can form an active Z-ring, and reveals the amino acid transporter BraB as a new cell division influencing factor. |
| title_fullStr | Minimization of the Bacillus subtilis divisome suggests FtsZ and SepF can form an active Z-ring, and reveals the amino acid transporter BraB as a new cell division influencing factor. |
| title_full_unstemmed | Minimization of the Bacillus subtilis divisome suggests FtsZ and SepF can form an active Z-ring, and reveals the amino acid transporter BraB as a new cell division influencing factor. |
| title_short | Minimization of the Bacillus subtilis divisome suggests FtsZ and SepF can form an active Z-ring, and reveals the amino acid transporter BraB as a new cell division influencing factor. |
| title_sort | minimization of the bacillus subtilis divisome suggests ftsz and sepf can form an active z ring and reveals the amino acid transporter brab as a new cell division influencing factor |
| url | https://doi.org/10.1371/journal.pgen.1011567 |
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