• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of pnasPNASInfo for AuthorsSubscriptionsAboutThis Article
Proc Natl Acad Sci U S A. Feb 1, 1993; 90(3): 1053–1057.

Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein.


FtsZ is an essential cell division protein in Escherichia coli that forms a ring structure at the division site under cell cycle control. The dynamic nature of the FtsZ ring suggests possible similarities to eukaryotic filament forming proteins such as tubulin. In this study we have determined that FtsZ is a GTP/GDP binding protein with GTPase activity. A short segment of FtsZ is homologous to a segment in tubulin believed to be involved in the interaction between tubulin and guanine nucleotides. A lethal ftsZ mutation, ftsZ3 (Rsa), that leads to an amino acid alteration in this homologous segment decreased GTP binding and hydrolysis, suggesting that interaction with GTP is essential for ftsZ function.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.2M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Dai K, Lutkenhaus J. ftsZ is an essential cell division gene in Escherichia coli. J Bacteriol. 1991 Jun;173(11):3500–3506. [PMC free article] [PubMed]
  • Wang XD, de Boer PA, Rothfield LI. 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):3363–3372. [PMC free article] [PubMed]
  • Pla J, Sánchez M, Palacios P, Vicente M, Aldea M. Preferential cytoplasmic location of FtsZ, a protein essential for Escherichia coli septation. Mol Microbiol. 1991 Jul;5(7):1681–1686. [PubMed]
  • Yi QM, Rockenbach S, Ward JE, Jr, Lutkenhaus J. Structure and expression of the cell division genes ftsQ, ftsA and ftsZ. J Mol Biol. 1985 Aug 5;184(3):399–412. [PubMed]
  • Tétart F, Bouché JP. Regulation of the expression of the cell-cycle gene ftsZ by DicF antisense RNA. Division does not require a fixed number of FtsZ molecules. Mol Microbiol. 1992 Mar;6(5):615–620. [PubMed]
  • Begg KJ, Donachie WD. Cell shape and division in Escherichia coli: experiments with shape and division mutants. J Bacteriol. 1985 Aug;163(2):615–622. [PMC free article] [PubMed]
  • Taschner PE, Huls PG, Pas E, Woldringh CL. Division behavior and shape changes in isogenic ftsZ, ftsQ, ftsA, pbpB, and ftsE cell division mutants of Escherichia coli during temperature shift experiments. J Bacteriol. 1988 Apr;170(4):1533–1540. [PMC free article] [PubMed]
  • Lutkenhaus JF. Coupling of DNA replication and cell division: sulB is an allele of ftsZ. J Bacteriol. 1983 Jun;154(3):1339–1346. [PMC free article] [PubMed]
  • Bi E, Lutkenhaus J. Analysis of ftsZ mutations that confer resistance to the cell division inhibitor SulA (SfiA). J Bacteriol. 1990 Oct;172(10):5602–5609. [PMC free article] [PubMed]
  • de Boer PA, Crossley RE, Rothfield LI. Central role for the Escherichia coli minC gene product in two different cell division-inhibition systems. Proc Natl Acad Sci U S A. 1990 Feb;87(3):1129–1133. [PMC free article] [PubMed]
  • Bi E, Lutkenhaus J. Interaction between the min locus and ftsZ. J Bacteriol. 1990 Oct;172(10):5610–5616. [PMC free article] [PubMed]
  • Bi EF, Lutkenhaus J. FtsZ ring structure associated with division in Escherichia coli. Nature. 1991 Nov 14;354(6349):161–164. [PubMed]
  • Korn ED, Carlier MF, Pantaloni D. Actin polymerization and ATP hydrolysis. Science. 1987 Oct 30;238(4827):638–644. [PubMed]
  • Weisenberg RC. Microtubule formation in vitro in solutions containing low calcium concentrations. Science. 1972 Sep 22;177(4054):1104–1105. [PubMed]
  • Hesse J, Thierauf M, Ponstingl H. Tubulin sequence region beta 155-174 is involved in binding exchangeable guanosine triphosphate. J Biol Chem. 1987 Nov 15;262(32):15472–15475. [PubMed]
  • Sternlicht H, Yaffe MB, Farr GW. A model of the nucleotide-binding site in tubulin. FEBS Lett. 1987 Apr 20;214(2):226–235. [PubMed]
  • Fürste JP, Pansegrau W, Frank R, Blöcker H, Scholz P, Bagdasarian M, Lanka E. Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene. 1986;48(1):119–131. [PubMed]
  • Manne V, Bekesi E, Kung HF. Ha-ras proteins exhibit GTPase activity: point mutations that activate Ha-ras gene products result in decreased GTPase activity. Proc Natl Acad Sci U S A. 1985 Jan;82(2):376–380. [PMC free article] [PubMed]
  • Siekierka J, Manne V, Mauser L, Ochoa S. Polypeptide chain initiation in eukaryotes: reversibility of the ternary complex-forming reaction. Proc Natl Acad Sci U S A. 1983 Mar;80(5):1232–1235. [PMC free article] [PubMed]
  • Manne V, Yamazaki S, Kung HF. Guanosine nucleotide binding by highly purified Ha-ras-encoded p21 protein produced in Escherichia coli. Proc Natl Acad Sci U S A. 1984 Nov;81(22):6953–6957. [PMC free article] [PubMed]
  • Schmitt HD, Wagner P, Pfaff E, Gallwitz D. The ras-related YPT1 gene product in yeast: a GTP-binding protein that might be involved in microtubule organization. Cell. 1986 Nov 7;47(3):401–412. [PubMed]
  • Serafini T, Orci L, Amherdt M, Brunner M, Kahn RA, Rothman JE. ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein. Cell. 1991 Oct 18;67(2):239–253. [PubMed]
  • Bourne HR, Sanders DA, McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature. 1991 Jan 10;349(6305):117–127. [PubMed]
  • Zylicz M, LeBowitz JH, McMacken R, Georgopoulos C. The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system. Proc Natl Acad Sci U S A. 1983 Nov;80(21):6431–6435. [PMC free article] [PubMed]
  • Jacobs M, Smith H, Taylor EW. Tublin: nucleotide binding and enzymic activity. J Mol Biol. 1974 Nov 5;89(3):455–468. [PubMed]
  • Geahlen RL, Haley BE. Use of a GTP photoaffinity probe to resolve aspects of the mechanism of tubulin polymerization. J Biol Chem. 1979 Dec 10;254(23):11982–11987. [PubMed]
  • Carlier MF. Guanosine-5'-triphosphate hydrolysis and tubulin polymerization. Review article. Mol Cell Biochem. 1982 Sep 3;47(2):97–113. [PubMed]
  • Viitanen PV, Lubben TH, Reed J, Goloubinoff P, O'Keefe DP, Lorimer GH. Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent. Biochemistry. 1990 Jun 19;29(24):5665–5671. [PubMed]
  • Burns RG. Alpha-, beta-, and gamma-tubulins: sequence comparisons and structural constraints. Cell Motil Cytoskeleton. 1991;20(3):181–189. [PubMed]
  • Yi QM, Lutkenhaus J. The nucleotide sequence of the essential cell-division gene ftsZ of Escherichia coli. Gene. 1985;36(3):241–247. [PubMed]
  • Beall B, Lowe M, Lutkenhaus J. Cloning and characterization of Bacillus subtilis homologs of Escherichia coli cell division genes ftsZ and ftsA. J Bacteriol. 1988 Oct;170(10):4855–4864. [PMC free article] [PubMed]
  • Margolin W, Corbo JC, Long SR. Cloning and characterization of a Rhizobium meliloti homolog of the Escherichia coli cell division gene ftsZ. J Bacteriol. 1991 Sep;173(18):5822–5830. [PMC free article] [PubMed]
  • Linse K, Mandelkow EM. The GTP-binding peptide of beta-tubulin. Localization by direct photoaffinity labeling and comparison with nucleotide-binding proteins. J Biol Chem. 1988 Oct 15;263(29):15205–15210. [PubMed]
  • Bukau B, Walker GC. Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism. J Bacteriol. 1989 May;171(5):2337–2346. [PMC free article] [PubMed]
  • Bi E, Lutkenhaus J. Isolation and characterization of ftsZ alleles that affect septal morphology. J Bacteriol. 1992 Aug;174(16):5414–5423. [PMC free article] [PubMed]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences


Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...


Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...