Nucleoid occlusion factor SlmA is a DNA-activated FtsZ polymerization antagonist

The tubulin-like FtsZ protein initiates assembly of the bacterial cytokinetic machinery by polymerizing into a ring structure, the Z ring, at the prospective site of division. To block Z-ring formation over the nucleoid and help coordinate cell division with chromosome segregation, Escherichia coli...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2011-03, Vol.108 (9), p.3773-3778
Main Authors: Cho, Hongbaek, McManus, Heather R., Dove, Simon L., Bernhardt, Thomas G., Silhavy, Thomas J.
Format: Article
Language:English
Subjects:
Bacterial Proteins - antagonists & inhibitors
Bacterial Proteins - metabolism
Bacterial Proteins - ultrastructure
Base Sequence
Binding Sites
Biological Sciences
Carrier Proteins - metabolism
Cell division
Cell separation
Chromatin
Chromosomes
Chromosomes, Bacterial - metabolism
Cytoskeletal Proteins - antagonists & inhibitors
Cytoskeletal Proteins - metabolism
Cytoskeletal Proteins - ultrastructure
Daughter cells
Deoxyribonucleic acid
DNA
DNA, Bacterial - metabolism
DNA-Binding Proteins - metabolism
E coli
Escherichia coli
Escherichia coli - metabolism
Escherichia coli Proteins - metabolism
FtsZ protein
Gene expression regulation
Immunoprecipitation
Models, Biological
Molecular Sequence Data
Nucleoids
Occlusion
Polymerization
Polymers
Protein Binding
Proteins
Replication origin
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Summary:The tubulin-like FtsZ protein initiates assembly of the bacterial cytokinetic machinery by polymerizing into a ring structure, the Z ring, at the prospective site of division. To block Z-ring formation over the nucleoid and help coordinate cell division with chromosome segregation, Escherichia coli employs the nucleoid-associated division inhibitor, SlmA. Here, we investigate the mechanism by which SlmA regulates FtsZ assembly. We show that SlmA disassembles FtsZ polymers in vitro. In addition, using chromatin ¡mmunoprecipitation (ChIP), we identified 24 SlmA-binding sequences (SBSs) on the chromosome. Remarkably, SlmA binding to SBSs dramatically enhanced its ability to interfere with FtsZ polymerization, and ChIP studies indicate that SlmA regulates FtsZ assembly at these sites in vivo. Because of the dynamic and highly organized nature of the chromosome, coupling SlmA activation to specific DNA binding provides a mechanism for the precise spatiotemporal control of its anti-FtsZ activity within the cell.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1018674108