Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC

I.F.F. de Oliveira, A. Sousa Borges, V. Kooij, J. Bartosiak-Jentys, S. Luirink, D.J. Scheffers

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

Background: 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. Methodology/Principal Findings: 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. Conclusions/Significance: 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. © 2010 de Oliveira et al.
LanguageEnglish
Pagese12048-e12057
Number of pages10
JournalPLoS ONE
Volume5
Issue number8
DOIs
Publication statusPublished - 2010

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Bacilli
Bacillus subtilis
Cell Division
Cells
mutation
cell division
Polymerization
mutants
Mutation
polymerization
Guanosine Triphosphate
Hydrolysis
Poles
Proteins
lethal genes
proteins
hydrolysis
cells
methodology

Bibliographical note

e12048

Cite this

de Oliveira, I. F. F., Sousa Borges, A., Kooij, V., Bartosiak-Jentys, J., Luirink, S., & Scheffers, D. J. (2010). Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. PLoS ONE, 5(8), e12048-e12057. https://doi.org/10.1371/journal.pone.0012048
de Oliveira, I.F.F. ; Sousa Borges, A. ; Kooij, V. ; Bartosiak-Jentys, J. ; Luirink, S. ; Scheffers, D.J. / Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. In: PLoS ONE. 2010 ; Vol. 5, No. 8. pp. e12048-e12057.
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abstract = "Background: 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. Methodology/Principal Findings: 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. Conclusions/Significance: 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. {\circledC} 2010 de Oliveira et al.",
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de Oliveira, IFF, Sousa Borges, A, Kooij, V, Bartosiak-Jentys, J, Luirink, S & Scheffers, DJ 2010, 'Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC', PLoS ONE, vol. 5, no. 8, pp. e12048-e12057. https://doi.org/10.1371/journal.pone.0012048

Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. / de Oliveira, I.F.F.; Sousa Borges, A.; Kooij, V.; Bartosiak-Jentys, J.; Luirink, S.; Scheffers, D.J.

In: PLoS ONE, Vol. 5, No. 8, 2010, p. e12048-e12057.

Research output: Contribution to JournalArticleAcademicpeer-review

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AU - de Oliveira, I.F.F.

AU - Sousa Borges, A.

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AU - Luirink, S.

AU - Scheffers, D.J.

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N2 - Background: 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. Methodology/Principal Findings: 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. Conclusions/Significance: 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. © 2010 de Oliveira et al.

AB - Background: 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. Methodology/Principal Findings: 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. Conclusions/Significance: 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. © 2010 de Oliveira et al.

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JO - PLoS ONE

T2 - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

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de Oliveira IFF, Sousa Borges A, Kooij V, Bartosiak-Jentys J, Luirink S, Scheffers DJ. Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC. PLoS ONE. 2010;5(8):e12048-e12057. https://doi.org/10.1371/journal.pone.0012048