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PMID:22056926

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Citation

Galli, E and Gerdes, K (2012) FtsZ-ZapA-ZapB interactome of Escherichia coli. J. Bacteriol. 194:292-302

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 CaCl(2), 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.

Links

PubMed PMC3256659 Online version:10.1128/JB.05821-11

Keywords

Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Carrier Proteins/genetics; Carrier Proteins/metabolism; Cell Cycle Proteins/genetics; Cell Cycle Proteins/metabolism; Cytokinesis; Cytoskeletal Proteins/genetics; Cytoskeletal Proteins/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Bacterial/physiology; Green Fluorescent Proteins; Hydrogen-Ion Concentration; Mutation; Plasmids; Time Factors

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:ZAPA

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0AF36

F

Seeded From UniProt

complete

ECOLI:ZAPB

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0ADS2

F

Seeded From UniProt

complete

ECOLI:FTSZ

GO:0003924: GTPase activity

ECO:0000315:

F

FIG 2 Deletion of ZapB specifically reduces FtsZ division potential. Overnight cultures of TS mutant strains were grown to equal density in LB medium at 30°C and serially diluted (10−1 to 10−6) in LB medium. Aliquots (10 μl) were spotted on NA plates incubated at 30°C overnight.

complete
CACAO 3969


See also

References

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