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Mol Microbiol. 2017 May;104(4):652-663. doi: 10.1111/mmi.13655. Epub 2017 Mar 26.

ZapA and ZapB form an FtsZ-independent structure at midcell.

Author information

1
Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA, 02115, USA.
2
Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, MD, 21205, USA.

Abstract

Cell division in Escherichia coli begins with the polymerization of FtsZ into a ring-like structure, the Z-ring, at midcell. All other division proteins are thought to require the Z-ring for recruitment to the future division site. Here, it is reported that the Z-ring associated proteins ZapA and ZapB form FtsZ-independent structures at midcell. Upon Z-ring disruption by the FtsZ polymerization antagonist SulA, ZapA remained at midcell as a cloud-like accumulation. Using ZapA(N60Y), a variant defective for interaction with FtsZ, it was established that these ZapA structures form without a connection to the Z-ring. Furthermore, midcell accumulations of GFP-ZapA(N60Y) often preceded Z-rings at midcell and required ZapB to assemble, suggesting that ZapB polymers form the foundation of these structures. In the absence of MatP, a DNA-binding protein that links ZapB to the chromosomal terminus region, cloud-like ZapA structures still formed but failed to track with the chromosome terminus and did not consistently precede FtsZ at midcell. Taken together, the results suggest that FtsZ-independent structures of ZapA-ZapB provide additional positional cues for Z-ring formation and may help coordinate its assembly with chromosome replication and segregation.

PMID:
28249098
PMCID:
PMC5426985
DOI:
10.1111/mmi.13655
[Indexed for MEDLINE]
Free PMC Article

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