MinC N- and C-Domain Interactions Modulate FtsZ Assembly, Division Site Selection, and MinD-Dependent Oscillation in Escherichia coli | Zendy

Christopher J. LaBreck | Zendy; Joseph Conti | Zendy; Marissa G. Viola | Zendy; Jodi L. Camberg | Zendy

Open Access

MinC N- and C-Domain Interactions Modulate FtsZ Assembly, Division Site Selection, and MinD-Dependent Oscillation in Escherichia coli

Author(s) -

Christopher J. LaBreck,

Joseph Conti,

Marissa G. Viola,

Jodi L. Camberg

Publication year - 2018

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.00374-18

Subject(s) - ftsz , biology , cell division , microbiology and biotechnology , mutant , mutagenesis , biochemistry , cell , gene

Bacterial cell division proceeds through the coordinated assembly of the FtsZ-ring, or Z-ring, at the site of division. Assembly of the Z-ring requires polymerization of FtsZ, which is regulated by several proteins in the cell. InEscherichia coli , the Min system, which contains MinC, MinD, and MinE proteins, exhibits polar oscillation and inhibits the assembly of FtsZ at nonseptal locations. Here, we identify regions on the surface of MinC that are important for contacting FtsZ and destabilizing FtsZ polymers.

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