Home LiteratureArticle Details
PMID: 12896999 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

In vivo characterization of Escherichia coli ftsZ mutants: effects on Z-ring structure and function.

Journal of bacteriology ·Vol. 185 ·No. 16 ·2003-08-00 ·Pages 4796-805

Stricker J, Erickson HP

Abstract

We have characterized the in vivo phenotypes of 17 mutations of Escherichia coli ftsZ. In particular, we determined whether these mutations can complement a null ftsZ phenotype, and we demonstrated that two noncomplementing mutations show partial dominant-negative behavior. We performed immunofluorescence microscopy to determine whether these mutants could assemble into normal or abnormal structures in vivo. The mutants separated into four classes-those that complemented the null and formed normal FtsZ rings, those that complemented the null but formed aberrant FtsZ structures, those that formed aberrant FtsZ structures and did not complement, and those that were unable to form any FtsZ structures. We did not find any mutations that produced nonfunctional Z rings of normal appearance. Surprisingly, some mutants that produced extensively spiraled Z-ring structures divided and grew with a normal doubling time. The analysis was carried out using a complementation system based on an ftsZ deletion strain, a temperature-sensitive rescue plasmid, and a complementation vector that placed mutated ftsZ alleles under the control of the pBAD promoter, which offered several advantages over previous systems.

MeSH Terms
Bacterial Proteins/genetics,metabolism Cell Division Culture Media Cytoskeletal Proteins Escherichia coli/cytology,genetics,growth & development,ultrastructure Genetic Complementation Test Microscopy, Fluorescence Mutation
Chemicals
Bacterial Proteins Culture Media Cytoskeletal Proteins FtsZ protein, Bacteria
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Stricker Jesse
Department of Cell Biology, Duke University Medical Center, Durham, North Carolina, USA.
Erickson Harold P
References (31)
31 references, click to expand
  1. Genetic and functional analyses of the conserved C-terminal core domain of Escherichia coli FtsZ.
    J Bacteriol. 1999 Dec;181(24):7531-44 PMID: 10601211
  2. Localization and function of early cell division proteins in filamentous Escherichia coli cells lacking phosphatidylethanolamine.
    J Bacteriol. 1998 Aug;180(16):4252-7 PMID: 9696776
  3. A set of ftsZ mutants blocked at different stages of cell division in Caulobacter.
    Mol Microbiol. 2001 Apr;40(2):347-60 PMID: 11309118
  4. Unique and overlapping roles for ZipA and FtsA in septal ring assembly in Escherichia coli.
    EMBO J. 2002 Feb 15;21(4):685-93 PMID: 11847116
  5. Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching.
    Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):3171-5 PMID: 11854462
  6. Asymmetric cell division in B. subtilis involves a spiral-like intermediate of the cytokinetic protein FtsZ.
    Cell. 2002 Apr 19;109(2):257-66 PMID: 12007411
  7. Site-specific mutations of FtsZ--effects on GTPase and in vitro assembly.
    BMC Microbiol. 2001;1:7 PMID: 11394965
  8. The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites.
    Proc Natl Acad Sci U S A. 1974 Apr;71(4):1342-6 PMID: 4598299
  9. Organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus (ftsZ).
    J Bacteriol. 1980 May;142(2):615-20 PMID: 6991482
  10. A 37 X 10(3) molecular weight plasmid-encoded protein is required for replication and copy number control in the plasmid pSC101 and its temperature-sensitive derivative pHS1.
    J Mol Biol. 1984 May 25;175(3):331-48 PMID: 6327996
  11. A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors.
    Gene. 1984 Nov;31(1-3):165-71 PMID: 6098521
  12. Cell division control in Escherichia coli K-12: some properties of the ftsZ84 mutation and suppression of this mutation by the product of a newly identified gene.
    J Bacteriol. 1988 Sep;170(9):4338-42 PMID: 2842315
  13. ftsZ is an essential cell division gene in Escherichia coli.
    J Bacteriol. 1991 Jun;173(11):3500-6 PMID: 2045370
  14. A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli.
    EMBO J. 1991 Nov;10(11):3363-72 PMID: 1915297
  15. FtsZ ring structure associated with division in Escherichia coli.
    Nature. 1991 Nov 14;354(6349):161-4 PMID: 1944597
  16. Isolation and characterization of ftsZ alleles that affect septal morphology.
    J Bacteriol. 1992 Aug;174(16):5414-23 PMID: 1644768
  17. Guanine nucleotide-dependent assembly of FtsZ into filaments.
    J Bacteriol. 1994 May;176(9):2754-8 PMID: 8169229
  18. GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules.
    Proc Natl Acad Sci U S A. 1994 Jun 21;91(13):5813-7 PMID: 8016071
  19. Use of immunofluorescence to visualize cell-specific gene expression during sporulation in Bacillus subtilis.
    J Bacteriol. 1995 Jun;177(12):3386-93 PMID: 7768847
  20. Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter.
    J Bacteriol. 1995 Jul;177(14):4121-30 PMID: 7608087
  21. Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers.
    Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):519-23 PMID: 8552673
  22. FtsZ ring formation in fts mutants.
    J Bacteriol. 1996 Jul;178(13):3877-84 PMID: 8682793
  23. Visualization of the subcellular location of sporulation proteins in Bacillus subtilis using immunofluorescence microscopy.
    Mol Microbiol. 1995 Nov;18(3):459-70 PMID: 8748030
  24. 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 PMID: 8917533
  25. FtsZ-spirals and -arcs determine the shape of the invaginating septa in some mutants of Escherichia coli.
    Mol Microbiol. 1996 Oct;22(2):231-7 PMID: 8930908
  26. Temperature shift experiments with an ftsZ84(Ts) strain reveal rapid dynamics of FtsZ localization and indicate that the Z ring is required throughout septation and cannot reoccupy division sites once constriction has initiated.
    J Bacteriol. 1997 Jul;179(13):4277-84 PMID: 9209044
  27. Gene expression from plasmids containing the araBAD promoter at subsaturating inducer concentrations represents mixed populations.
    Proc Natl Acad Sci U S A. 1997 Jul 22;94(15):8168-72 PMID: 9223333
  28. Analysis of the interaction of FtsZ with itself, GTP, and FtsA.
    J Bacteriol. 1997 Sep;179(17):5551-9 PMID: 9287012
  29. Crystal structure of the bacterial cell-division protein FtsZ.
    Nature. 1998 Jan 8;391(6663):203-6 PMID: 9428770
  30. FtsZ from Escherichia coli, Azotobacter vinelandii, and Thermotoga maritima--quantitation, GTP hydrolysis, and assembly.
    Cell Motil Cytoskeleton. 1998;40(1):71-86 PMID: 9605973
  31. Straight and curved conformations of FtsZ are regulated by GTP hydrolysis.
    J Bacteriol. 2000 Jan;182(1):164-70 PMID: 10613876
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
2003-08-00
Pages
4796-805
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC166488
Subset
IM
Grants
NIGMS NIH HHS · GM28553 · United States
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]