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Genetic and biochemical characterization of the MinC-FtsZ interaction in Bacillus subtilis.
- Source :
-
PloS one [PLoS One] 2013; Vol. 8 (4), pp. e60690. Date of Electronic Publication: 2013 Apr 05. - Publication Year :
- 2013
-
Abstract
- Cell division in bacteria is regulated by proteins that interact with FtsZ and modulate its ability to polymerize into the Z ring structure. The best studied of these regulators is MinC, an inhibitor of FtsZ polymerization that plays a crucial role in the spatial control of Z ring formation. Recent work established that E. coli MinC interacts with two regions of FtsZ, the bottom face of the H10 helix and the extreme C-terminal peptide (CTP). Here we determined the binding site for MinC on Bacillus subtilis FtsZ. Selection of a library of FtsZ mutants for survival in the presence of Min overexpression resulted in the isolation of 13 Min-resistant mutants. Most of the substitutions that gave rise to Min resistance clustered around the H9 and H10 helices in the C-terminal domain of FtsZ. In addition, a mutation in the CTP of B. subtilis FtsZ also produced MinC resistance. Biochemical characterization of some of the mutant proteins showed that they exhibited normal polymerization properties but reduced interaction with MinC, as expected for binding site mutations. Thus, our study shows that the overall architecture of the MinC-FtsZ interaction is conserved in E. coli and B. subtilis. Nevertheless, there was a clear difference in the mutations that conferred Min resistance, with those in B. subtilis FtsZ pointing to the side of the molecule rather than to its polymerization interface. This observation suggests that the mechanism of Z ring inhibition by MinC differs in both species.
- Subjects :
- Bacillus subtilis drug effects
Bacterial Proteins chemistry
Bacterial Proteins genetics
Binding Sites
Cytoskeletal Proteins chemistry
Cytoskeletal Proteins genetics
Drug Resistance, Bacterial genetics
Escherichia coli genetics
Escherichia coli metabolism
Models, Molecular
Mutation
Protein Binding
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Secondary
Bacillus subtilis genetics
Bacillus subtilis metabolism
Bacterial Proteins metabolism
Cytoskeletal Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1932-6203
- Volume :
- 8
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- PloS one
- Publication Type :
- Academic Journal
- Accession number :
- 23577149
- Full Text :
- https://doi.org/10.1371/journal.pone.0060690