PMID:23577149

Citation	Blasios, V, Bisson-Filho, AW, Castellen, P, Nogueira, ML, Bettini, J, Portugal, RV, Zeri, AC and Gueiros-Filho, FJ (2013) Genetic and Biochemical Characterization of the MinC-FtsZ Interaction in Bacillus subtilis. PLoS ONE 8:e60690
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.
Links	PubMed Online version:10.1371/journal.pone.0060690
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
BACSU:FTSZ		GO:0003924: GTPase activity	ECO:0000314:		F		supplement figure 6	complete CACAO 8163
BACSU:FTSZ		GO:0005515: protein binding	ECO:0000021:	UniProtKB:Q01463	F		Figure 5	complete CACAO 8164
BACSU:FTSZ	enables	GO:0003924: GTPase activity	ECO:0000314: direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
BACSU:MINC		GO:0032272: negative regulation of protein polymerization	ECO:0000314:		P		Figure 4	complete CACAO 8165
BACSU:MINC	involved_in	GO:0032272: negative regulation of protein polymerization	ECO:0000314: direct assay evidence used in manual assertion		P		Seeded From UniProt	complete

References

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