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FtsZ-ZapA-ZapB Interactome of Escherichia coli

Lookup NU author(s): Elisa Galli, Professor Kenn Gerdes

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Abstract

Bacterial cell division relies on the formation and contraction of the Z ring, coordinated and regulated by a dynamic protein complex called the divisome. The cell division factor ZapA interacts directly with FtsZ and thereby increases FtsZ protofilament association and Z-ring stability. Here, we investigated ZapB interaction with ZapA and its effect on Z-ring formation and FtsZ protofilament bundling. The combination of the ftsZ84 allele that encodes an FtsZ variant that polymerizes inefficiently with a zapB null mutant resulted in a synthetic defective phenotype. Overproduction of ZapA led to the formation of aberrant FtsZ helical structures and delocalization of ZapB. The N-terminal end of ZapB was essential for ZapB-ZapA interaction, and amino acid changes close to the N terminus of ZapB exhibited reduced interaction with ZapA. Sedimentation assays showed that ZapB interacts strongly with ZapA and reduces ZapA's interaction with FtsZ in vitro. The morphology of the structures formed by ZapA and ZapB together was similar to the cables formed by ZapB in the presence of CaCl2, a known ZapB bundling agent. The in vivo and in vitro data support a model in which ZapA interacts strongly with ZapB and the ZapA-ZapB interaction is favored over ZapA-FtsZ.


Publication metadata

Author(s): Galli E, Gerdes K

Publication type: Article

Publication status: Published

Journal: Journal of Bacteriology

Year: 2012

Volume: 194

Issue: 2

Pages: 292-302

Print publication date: 01/01/2012

ISSN (print): 0021-9193

ISSN (electronic): 1098-5530

Publisher: American Society for Microbiology

URL: http://dx.doi.org/10.1128/JB.05821-11

DOI: 10.1128/JB.05821-11


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