Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC.
Cell division in Bacillus subtilis occurs precisely at midcell. Positional control of cell division is exerted by two mechanisms: nucleoid occlusion, through Noc, which prevents division through nucleoids, and the Min system, where the combined action of the MinC, D and J proteins prevents formation...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2010-08-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC2920321?pdf=render |
| _version_ | 1828524260454301696 |
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| author | Inês Filipa Fernandes de Oliveira Anabela de Sousa Borges Viola Kooij Jeremy Bartosiak-Jentys Joen Luirink Dirk-Jan Scheffers |
| author_facet | Inês Filipa Fernandes de Oliveira Anabela de Sousa Borges Viola Kooij Jeremy Bartosiak-Jentys Joen Luirink Dirk-Jan Scheffers |
| author_sort | Inês Filipa Fernandes de Oliveira |
| collection | DOAJ |
| description | Cell division in Bacillus subtilis occurs precisely at midcell. Positional control of cell division is exerted by two mechanisms: nucleoid occlusion, through Noc, which prevents division through nucleoids, and the Min system, where the combined action of the MinC, D and J proteins prevents formation of the FtsZ ring at cell poles or recently completed division sites.We used a genetic screen to identify mutations in ftsZ that confer resistance to the lethal overexpression of the MinC/MinD division inhibitor. The FtsZ mutants were purified and found to polymerize to a similar or lesser extent as wild type FtsZ, and all mutants displayed reduced GTP hydrolysis activity indicative of a reduced polymerization turnover. We found that even though the mutations conferred in vivo resistance to MinC/D, the purified FtsZ mutants did not display strong resistance to MinC in vitro.Our results show that in B. subtilis, overproduction of MinC can be countered by mutations that alter FtsZ polymerization dynamics. Even though it would be very likely that the FtsZ mutants found depend on other Z-ring stabilizing proteins such as ZapA, FtsA or SepF, we found this not to be the case. This indicates that the cell division process in B. subtilis is extremely robust. |
| first_indexed | 2024-12-11T20:44:14Z |
| format | Article |
| id | doaj.art-3aaa1c52feac4fb9b1fa5690e768b48a |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T20:44:14Z |
| publishDate | 2010-08-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-3aaa1c52feac4fb9b1fa5690e768b48a2022-12-22T00:51:25ZengPublic Library of Science (PLoS)PLoS ONE1932-62032010-08-0158e1204810.1371/journal.pone.0012048Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC.Inês Filipa Fernandes de OliveiraAnabela de Sousa BorgesViola KooijJeremy Bartosiak-JentysJoen LuirinkDirk-Jan ScheffersCell division in Bacillus subtilis occurs precisely at midcell. Positional control of cell division is exerted by two mechanisms: nucleoid occlusion, through Noc, which prevents division through nucleoids, and the Min system, where the combined action of the MinC, D and J proteins prevents formation of the FtsZ ring at cell poles or recently completed division sites.We used a genetic screen to identify mutations in ftsZ that confer resistance to the lethal overexpression of the MinC/MinD division inhibitor. The FtsZ mutants were purified and found to polymerize to a similar or lesser extent as wild type FtsZ, and all mutants displayed reduced GTP hydrolysis activity indicative of a reduced polymerization turnover. We found that even though the mutations conferred in vivo resistance to MinC/D, the purified FtsZ mutants did not display strong resistance to MinC in vitro.Our results show that in B. subtilis, overproduction of MinC can be countered by mutations that alter FtsZ polymerization dynamics. Even though it would be very likely that the FtsZ mutants found depend on other Z-ring stabilizing proteins such as ZapA, FtsA or SepF, we found this not to be the case. This indicates that the cell division process in B. subtilis is extremely robust.http://europepmc.org/articles/PMC2920321?pdf=render |
| spellingShingle | Inês Filipa Fernandes de Oliveira Anabela de Sousa Borges Viola Kooij Jeremy Bartosiak-Jentys Joen Luirink Dirk-Jan Scheffers Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. PLoS ONE |
| title | Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. |
| title_full | Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. |
| title_fullStr | Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. |
| title_full_unstemmed | Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. |
| title_short | Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. |
| title_sort | characterization of ftsz mutations that render bacillus subtilis resistant to minc |
| url | http://europepmc.org/articles/PMC2920321?pdf=render |
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