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A mutation in E scherichia coli fts Z bypasses the requirement for the essential division gene zip A and confers resistance to FtsZ assembly inhibitors by stabilizing protofilament bundling
Author(s) -
Haeusser Daniel P.,
Rowlett Veronica W.,
Margolin William
Publication year - 2015
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13081
Subject(s) - biology , mutation , gene , genetics
Summary The earliest step in E scherichia coli cell division consists of the assembly of FtsZ protein into a proto‐ring structure, tethered to the cytoplasmic membrane by FtsA and ZipA . The proto‐ring then recruits additional cell division proteins to form the divisome. Previously we described an ftsZ allele, ftsZ L169R , which maps to the side of the FtsZ subunit and confers resistance to FtsZ assembly inhibitory factors including K il of bacteriophage λ. Here we further characterize this allele and its mechanism of resistance. We found that FtsZ L169R permits the bypass of the normally essential ZipA , a property previously observed for FtsA gain‐of‐function mutants such as FtsA * or increased levels of the FtsA ‐interacting protein FtsN . Similar to FtsA *, FtsZ L169R also can partially suppress thermosensitive mutants of fts Q or fts K , which encode additional divisome proteins, and confers strong resistance to excess levels of FtsA , which normally inhibit FtsZ ring function. Additional genetic and biochemical assays provide further evidence that FtsZ L169R enhances FtsZ protofilament bundling, thereby conferring resistance to assembly inhibitors and bypassing the normal requirement for ZipA . This work highlights the importance of FtsZ protofilament bundling during cell division and its likely role in regulating additional divisome activities.