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Gene Review

ftsZ  -  GTP-binding tubulin-like cell division...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0096, JW0093, sfiB, sulB
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Disease relevance of ftsZ


Psychiatry related information on ftsZ


High impact information on ftsZ

  • The ftsZ gene in E. coli K-12 is an essential cell division gene [7].
  • Transcription of ftsZ oscillates during the cell cycle of Escherichia coli [8].
  • Transcriptional activity of the ftsZ promoters was found to be independent of DnaA, indicating that DNA replication and cell division may be independently controlled at the time when new rounds of DNA replication are initiated [8].
  • In addition, the sdiA gene product suppressed the action of other chromosomally encoded division inhibitors, induced minicell formation in wild type cells, and restored division activity to an ftsZ temperature-sensitive mutant grown under nonpermissive conditions [9].
  • The cell division ftsQAZ cluster and the ftsZ-dependent bolA morphogene of Escherichia coli are found to be driven by gearboxes, a distinct class of promoters characterized by showing an activity that is inversely dependent on growth rate [10].

Chemical compound and disease context of ftsZ


Biological context of ftsZ

  • The DNA sequence of a cloned segment of the Escherichia coli chromosome containing ftsQ, ftsA, and part of the ftsZ gene was determined and interpreted for genetic complementation and promoter fusion data for the region [16].
  • Amplification of a 2.6-kilobase chromosomal fragment of the mra region of Escherichia coli encompassing the ftsI(pbpB) gene and an open reading frame upstream with lethal to E. coli strains with mutations of the flanking cell division genes ftsQ, ftsA, and ftsZ [17].
  • The coupling between ftsZ transcription and initiation of DNA replication is not mediated by the DnaA-boxes upstream of ftsZ or by DnaA [18].
  • We show here that, although transcription from promoters upstream of ftsZ is increased when initiation of chromosome replication is blocked by DnaA inactivation, this response is not mediated by the DnaA-boxes near these promoters, nor is it specific to DnaA [18].
  • This response enables direct discrimination between phenotypes of sfiA and sfiB and moreover, also the selection of spontaneous mutants sfiA in a tif+ (recA+) genetic background [19].

Anatomical context of ftsZ


Associations of ftsZ with chemical compounds

  • Therefore, we investigated the response to the bacteriolytic beta-lactam cefsulodin of ftsZ and ftsI mutants growing at the restrictive (42 degrees C) temperature [22].
  • A sulB mutation leads to an altered ftsZ gene product which is slightly thermosensitive and has an altered mobility on polyacrylamide gels [23].
  • Introduction of the multicopy plasmid pZAQ containing the ftsZ gene, which is known to increase the level of FtsZ, suppressed the sensitivity of lon mutants to the DNA-damaging agents UV and nitrofurantoin [24].
  • After induction by anhydrotetracycline, expression of antisense ftsZ RNA resulted in generation of filamentous B. burgdorferi that were unable to divide and grew more slowly than uninduced cells [25].
  • The multicopy plasmid pZAQ, overproducing the septation proteins FtsZ, FtsA, and FtsQ, conferred amdinocillin resistance on a wild-type strain and suppressed the cell division inhibition in the leuS(Ts) delta (rodA-pbpA)::Kmr strain at 25 degrees C. The plasmid pAQ, in which the ftsZ gene is inactivated, did not confer amdinocillin resistance [26].

Regulatory relationships of ftsZ


Other interactions of ftsZ


Analytical, diagnostic and therapeutic context of ftsZ


  1. Regulation of Escherichia coli cell division genes ftsA and ftsZ by the two-component system rcsC-rcsB. Carballès, F., Bertrand, C., Bouché, J.P., Cam, K. Mol. Microbiol. (1999) [Pubmed]
  2. Ordered expression of ftsQA and ftsZ during the Caulobacter crescentus cell cycle. Sackett, M.J., Kelly, A.J., Brun, Y.V. Mol. Microbiol. (1998) [Pubmed]
  3. Identification, characterization, and chromosomal organization of the ftsZ gene from Brevibacterium lactofermentum. Honrubia, M.P., Fernández, F.J., Gil, J.A. Mol. Gen. Genet. (1998) [Pubmed]
  4. Identification of a new inhibitor of essential division gene ftsZ as the kil gene of defective prophage Rac. Conter, A., Bouché, J.P., Dassain, M. J. Bacteriol. (1996) [Pubmed]
  5. Characterization of ftsZ, the cell division gene of Buchnera aphidicola (endosymbiont of aphids) and detection of the product. Baumann, L., Baumann, P. Curr. Microbiol. (1998) [Pubmed]
  6. Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils. González, J.M., Vélez, M., Jiménez, M., Alfonso, C., Schuck, P., Mingorance, J., Vicente, M., Minton, A.P., Rivas, G. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  7. Overproduction of FtsZ induces minicell formation in E. coli. Ward, J.E., Lutkenhaus, J. Cell (1985) [Pubmed]
  8. Transcription of ftsZ oscillates during the cell cycle of Escherichia coli. Garrido, T., Sánchez, M., Palacios, P., Aldea, M., Vicente, M. EMBO J. (1993) [Pubmed]
  9. A factor that positively regulates cell division by activating transcription of the major cluster of essential cell division genes of Escherichia coli. Wang, X.D., de Boer, P.A., Rothfield, L.I. EMBO J. (1991) [Pubmed]
  10. Division genes in Escherichia coli are expressed coordinately to cell septum requirements by gearbox promoters. Aldea, M., Garrido, T., Pla, J., Vicente, M. EMBO J. (1990) [Pubmed]
  11. Control of ftsZ expression, cell division, and glutamine metabolism in Luria-Bertani medium by the alarmone ppGpp in Escherichia coli. Powell, B.S., Court, D.L. J. Bacteriol. (1998) [Pubmed]
  12. Cloning and characterization of a Rhizobium meliloti homolog of the Escherichia coli cell division gene ftsZ. Margolin, W., Corbo, J.C., Long, S.R. J. Bacteriol. (1991) [Pubmed]
  13. Analysis of the length distribution of murein glycan strands in ftsZ and ftsI mutants of E. coli. Ishidate, K., Ursinus, A., Höltje, J.V., Rothfield, L. FEMS Microbiol. Lett. (1998) [Pubmed]
  14. A cluster of four genes encoding enzymes for five steps in the folate biosynthetic pathway of Streptococcus pneumoniae. Lacks, S.A., Greenberg, B., Lopez, P. J. Bacteriol. (1995) [Pubmed]
  15. Escherichia coli cell division protein FtsZ is a guanine nucleotide binding protein. Mukherjee, A., Dai, K., Lutkenhaus, J. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  16. DNA sequence and transcriptional organization of essential cell division genes ftsQ and ftsA of Escherichia coli: evidence for overlapping transcriptional units. Robinson, A.C., Kenan, D.J., Hatfull, G.F., Sullivan, N.F., Spiegelberg, R., Donachie, W.D. J. Bacteriol. (1984) [Pubmed]
  17. Inhibition of growth of ftsQ, ftsA, and ftsZ mutant cells of Escherichia coli by amplification of a chromosomal region encompassing closely aligned cell division and cell growth genes. Jung, H.K., Ishino, F., Matsuhashi, M. J. Bacteriol. (1989) [Pubmed]
  18. The coupling between ftsZ transcription and initiation of DNA replication is not mediated by the DnaA-boxes upstream of ftsZ or by DnaA. Smith, R.W., McAteer, S., Masters, M. Mol. Microbiol. (1996) [Pubmed]
  19. Specific response of Escherichia coli K12 sfiA mutants to the presence of ethyl ester of N-alpha-palmitoyl-L-lysyl-L-lysine dihydrochloride (PLL) in a nutrient medium. Cegielska, A., Kupryszewski, G., Taylor, A. Mol. Gen. Genet. (1980) [Pubmed]
  20. Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers. Erickson, H.P., Taylor, D.W., Taylor, K.A., Bramhill, D. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  21. Vinblastine induces an interaction between FtsZ and tubulin in mammalian cells. Yu, X.C., Margolin, W., Gonzalez-Garay, M.L., Cabral, F. J. Cell. Sci. (1999) [Pubmed]
  22. Fast lysis of Escherichia coli filament cells requires differentiation of potential division sites. de Pedro, M.A., Höltje, J.V., Schwarz, H. Microbiology (Reading, Engl.) (2002) [Pubmed]
  23. Coupling of DNA replication and cell division: sulB is an allele of ftsZ. Lutkenhaus, J.F. J. Bacteriol. (1983) [Pubmed]
  24. Overproduction of FtsZ suppresses sensitivity of lon mutants to division inhibition. Lutkenhaus, J., Sanjanwala, B., Lowe, M. J. Bacteriol. (1986) [Pubmed]
  25. Borrelia burgdorferi ftsZ plays a role in cell division. Dubytska, L., Godfrey, H.P., Cabello, F.C. J. Bacteriol. (2006) [Pubmed]
  26. Penicillin-binding protein 2 inactivation in Escherichia coli results in cell division inhibition, which is relieved by FtsZ overexpression. Vinella, D., Joseleau-Petit, D., Thévenet, D., Bouloc, P., D'Ari, R. J. Bacteriol. (1993) [Pubmed]
  27. Regulation of the expression of the cell-cycle gene ftsZ by DicF antisense RNA. Division does not require a fixed number of FtsZ molecules. Tétart, F., Bouché, J.P. Mol. Microbiol. (1992) [Pubmed]
  28. Regulation and mode of action of the second small RNA activator of RpoS translation, RprA. Majdalani, N., Hernandez, D., Gottesman, S. Mol. Microbiol. (2002) [Pubmed]
  29. Role of sulA and sulB in filamentation by lon mutants of Escherichia coli K-12. Gottesman, S., Halpern, E., Trisler, P. J. Bacteriol. (1981) [Pubmed]
  30. Epitope mapping of Escherichia coli cell division protein FtsZ with monoclonal antibodies. Voskuil, J.L., Westerbeek, C.A., Wu, C., Kolk, A.H., Nanninga, N. J. Bacteriol. (1994) [Pubmed]
  31. Division behavior and shape changes in isogenic ftsZ, ftsQ, ftsA, pbpB, and ftsE cell division mutants of Escherichia coli during temperature shift experiments. Taschner, P.E., Huls, P.G., Pas, E., Woldringh, C.L. J. Bacteriol. (1988) [Pubmed]
  32. A murC gene from coryneform bacteria. Wachi, M., Wijayarathna, C.D., Teraoka, H., Nagai, K. Appl. Microbiol. Biotechnol. (1999) [Pubmed]
  33. Analysis of cell division gene ftsZ (sulB) from gram-negative and gram-positive bacteria. Corton, J.C., Ward, J.E., Lutkenhaus, J. J. Bacteriol. (1987) [Pubmed]
  34. Identification and semi-quantitative analysis of Mycobacterium tuberculosis H37Rv ftsZ gene-specific promoter activity-containing regions. Roy, S., Mir, M.A., Anand, S.P., Niederweis, M., Ajitkumar, P. Res. Microbiol. (2004) [Pubmed]
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