» Articles » PMID: 10449747

Identification and Characterization of a Negative Regulator of FtsZ Ring Formation in Bacillus Subtilis

Overview
Specialty Science
Date 1999 Aug 18
PMID 10449747
Citations 114
Authors
Affiliations
Soon will be listed here.
Abstract

During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. We have identified a regulator of FtsZ ring formation in Bacillus subtilis. This protein, EzrA, modulates the frequency and position of FtsZ ring formation. The loss of ezrA resulted in cells with multiple FtsZ rings located at polar as well as medial sites. Moreover, the critical concentration of FtsZ required for ring formation was lower in ezrA null mutants than in wild-type cells. EzrA was associated with the cell membrane and also colocalized with FtsZ to the nascent septal site. We propose that EzrA interacts either with FtsZ or with one of its binding partners to promote depolymerization.

Citing Articles

Two new enzymes that liberate undecaprenyl-phosphate to replenish the carrier lipid pool during envelope stress.

Roney I, Rudner D mBio. 2025; 16(3):e0371024.

PMID: 39878533 PMC: 11898649. DOI: 10.1128/mbio.03710-24.


Minimization of the Bacillus subtilis divisome suggests FtsZ and SepF can form an active Z-ring, and reveals the amino acid transporter BraB as a new cell division influencing factor.

Gulsoy I, Saaki T, Wenzel M, Syvertsson S, Morimoto T, Siersma T PLoS Genet. 2025; 21(1):e1011567.

PMID: 39869651 PMC: 11790237. DOI: 10.1371/journal.pgen.1011567.


Comprehensive double-mutant analysis of the envelope using double-CRISPRi.

Koo B, Todor H, Sun J, van Gestel J, Hawkins J, Hearne C bioRxiv. 2024; .

PMID: 39185233 PMC: 11343205. DOI: 10.1101/2024.08.14.608006.


Design-build-test of recombinant chassis cell by lifespan engineering for robust bioprocesses.

Ren K, Wang Q, Chen J, Zhang H, Guo Z, Xu M Synth Syst Biotechnol. 2024; 9(3):470-480.

PMID: 38634000 PMC: 11021899. DOI: 10.1016/j.synbio.2024.04.004.


FacZ is a GpsB-interacting protein that prevents aberrant division-site placement in Staphylococcus aureus.

Bartlett T, Sisley T, Mychack A, Walker S, Baker R, Rudner D Nat Microbiol. 2024; 9(3):801-813.

PMID: 38443581 PMC: 10914604. DOI: 10.1038/s41564-024-01607-y.


References
1.
Berger B, Wilson D, Wolf E, Tonchev T, Milla M, Kim P . Predicting coiled coils by use of pairwise residue correlations. Proc Natl Acad Sci U S A. 1995; 92(18):8259-63. PMC: 41136. DOI: 10.1073/pnas.92.18.8259. View

2.
Perego M, Spiegelman G, Hoch J . Structure of the gene for the transition state regulator, abrB: regulator synthesis is controlled by the spo0A sporulation gene in Bacillus subtilis. Mol Microbiol. 1988; 2(6):689-99. DOI: 10.1111/j.1365-2958.1988.tb00079.x. View

3.
Pogliano K, Harry E, Losick R . Visualization of the subcellular location of sporulation proteins in Bacillus subtilis using immunofluorescence microscopy. Mol Microbiol. 1995; 18(3):459-70. DOI: 10.1111/j.1365-2958.1995.mmi_18030459.x. View

4.
Gimeno R, Espenshade P, Kaiser C . SED4 encodes a yeast endoplasmic reticulum protein that binds Sec16p and participates in vesicle formation. J Cell Biol. 1995; 131(2):325-38. PMC: 2199979. DOI: 10.1083/jcb.131.2.325. View

5.
Lin D, Levin P, Grossman A . Bipolar localization of a chromosome partition protein in Bacillus subtilis. Proc Natl Acad Sci U S A. 1997; 94(9):4721-6. PMC: 20791. DOI: 10.1073/pnas.94.9.4721. View