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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Genetic and Biochemical Characterization of the MinC-FtsZ Interaction in Bacillus subtilis

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Author(s):
Blasios, Valdir [1] ; Bisson-Filho, Alexandre W. [1] ; Castellen, Patricia [1, 2] ; Nogueira, Maria Luiza C. [2] ; Bettini, Jefferson [3] ; Portugal, Rodrigo V. [3] ; Zeri, Ana Carolina M. [2] ; Gueiros-Filho, Frederico J. [1]
Total Authors: 8
Affiliation:
[1] Univ Sao Paulo, Inst Quim, Dept Bioquim, BR-01498 Sao Paulo - Brazil
[2] CNPEM, Brazilian Biosci Natl Lab LNBio, Campinas, SP - Brazil
[3] CNPEM, Nanotechnol Natl Lab LNNano, Campinas, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: PLoS One; v. 8, n. 4 APR 5 2013.
Web of Science Citations: 9
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. (AU)

FAPESP's process: 10/51866-0 - SMolBNet 2.0: combining genetics and NMR to dissect fundamental protein-protein interactions for complex bacterial division
Grantee:Frederico José Gueiros Filho
Support type: Regular Research Grants