Open AccessThe MinC component of the division site selection system in Escherichia coli interacts with FtsZ to prevent polymerization
Author(s) -
Zonglin Hu,
Amit Mukherjee,
Sébastien Pichoff,
Joe Lutkenhaus
Publication year - 1999
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.96.26.14819
Subject(s) - ftsz , cell division , gtpase , microbiology and biotechnology , escherichia coli , biology , chemistry , cell , biochemistry , gene
Positioning of the Z ring at the midcell site inEscherichia coli is assured by themin system, which masks polar sites through topological regulation of MinC, an inhibitor of division. To study how MinC inhibits division, we have generated a MalE-MinC fusion that retains full biological activity. We find that MalE-MinC interacts with FtsZ and prevents polymerization without inhibiting FtsZ's GTPase activity. MalE-MinC19 has reduced ability to inhibit division, reduced affinity for FtsZ, and reduced ability to inhibit FtsZ polymerization. These results, along with MinC localization, suggest that MinC rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings.