FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli
- PMID: 8930908
- DOI: 10.1046/j.1365-2958.1996.00100.x
FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli
Abstract
The essential cell division protein FtsZ forms a dynamic ring structure at the future division site. This Z-ring contracts during cell division while maintaining a position at the leading edge of the invaginating septum. Using immunofluorescence microscopy we have characterized two situations in which non-ring FtsZ structures are formed. In ftsZ26 (temperature sensitive, Ts) mutant cells, FtsZ-spirals are formed and lead to formation of spirally invaginating septa, which in turn cause morphological abnormalities. In rodAoul mutant cells, which grow as spheres instead of rods, FtsZ-arcs are formed where asymmetric septal invaginations are initiated. The FtsZ-arcs later mature into complete FtsZ-rings. Our data show that Z-spirals and Z-arcs can contract and that in doing so, they determine the shape of the invaginating septa. These results also strongly suggest that in normal cell division, FtsZ is positioned to a single nucleation site on the inner membrane, from which it polymerizes bidirectionally around the cell circumference to form the Z-ring.
Similar articles
-
Two polypeptide products of the Escherichia coli cell division gene ftsW and a possible role for FtsW in FtsZ function.J Bacteriol. 1997 Feb;179(3):784-93. doi: 10.1128/jb.179.3.784-793.1997. J Bacteriol. 1997. PMID: 9006034 Free PMC article.
-
In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function.J Bacteriol. 2003 Aug;185(16):4796-805. doi: 10.1128/JB.185.16.4796-4805.2003. J Bacteriol. 2003. PMID: 12896999 Free PMC article.
-
Colocalization of cell division proteins FtsZ and FtsA to cytoskeletal structures in living Escherichia coli cells by using green fluorescent protein.Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):12998-3003. doi: 10.1073/pnas.93.23.12998. Proc Natl Acad Sci U S A. 1996. PMID: 8917533 Free PMC article.
-
FtsZ: a novel target for tuberculosis drug discovery.Curr Top Med Chem. 2007;7(5):527-43. doi: 10.2174/156802607780059790. Curr Top Med Chem. 2007. PMID: 17346197 Review.
-
FtsZ ring in bacterial cytokinesis.Mol Microbiol. 1993 Aug;9(3):403-9. doi: 10.1111/j.1365-2958.1993.tb01701.x. Mol Microbiol. 1993. PMID: 8412689 Review.
Cited by
-
Dynamics of FtsZ assembly during sporulation in Streptomyces coelicolor A3(2).J Bacteriol. 2005 May;187(9):3227-37. doi: 10.1128/JB.187.9.3227-3237.2005. J Bacteriol. 2005. PMID: 15838050 Free PMC article.
-
Analysis of FtsZ assembly by light scattering and determination of the role of divalent metal cations.J Bacteriol. 1999 Feb;181(3):823-32. doi: 10.1128/JB.181.3.823-832.1999. J Bacteriol. 1999. PMID: 9922245 Free PMC article.
-
F-actin-like filaments formed by plasmid segregation protein ParM.EMBO J. 2002 Dec 16;21(24):6935-43. doi: 10.1093/emboj/cdf672. EMBO J. 2002. PMID: 12486014 Free PMC article.
-
Condensation of FtsZ filaments can drive bacterial cell division.Proc Natl Acad Sci U S A. 2009 Jan 6;106(1):121-6. doi: 10.1073/pnas.0807963106. Epub 2008 Dec 30. Proc Natl Acad Sci U S A. 2009. PMID: 19116281 Free PMC article.
-
Two Dictyostelium orthologs of the prokaryotic cell division protein FtsZ localize to mitochondria and are required for the maintenance of normal mitochondrial morphology.Eukaryot Cell. 2003 Dec;2(6):1315-26. doi: 10.1128/EC.2.6.1315-1326.2003. Eukaryot Cell. 2003. PMID: 14665465 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources