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Gene Review

ECs0093  -  cell division protein FtsW

Escherichia coli O157:H7 str. Sakai

 
 
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Disease relevance of ECs0093

  • Using gel renaturation, pull-down, and solid-phase assays, we confirm that FtsZ and FtsW interact through their C-terminal tails, which carry extensions absent in their Escherichia coli counterparts [1].
  • Interaction between FtsZ and FtsW of Mycobacterium tuberculosis [1].
  • After comparison with the recent topology of Streptococcus pneumoniae FtsW, we could identify all the fusions in absolute agreement with the predicted model: N-terminal and C-terminal ends in the cytoplasm, 10 transmembrane segments and one large loop of 67 amino acids (E240-E306) located in the periplasm [2].
 

High impact information on ECs0093

  • Crucial to these interactions is the cluster of aspartate residues Asp(367) to Asp(370) of FtsZ, which most likely interact with a cluster of positively charged residues in the C-terminal tail of FtsW [1].
  • We conclude that FtsW is an essential cell-division protein in Escherichia coli, and that it plays a role in the stabilization of the FtsZ ring during cell division [3].
  • However, in a simpler in vitro system using isolated membranes, acylation with cephalexin was not impaired by depletion of FtsW or FtsN [4].
  • Specifically, cephalexin acylated PBP3 about 50% faster in a population of dividing cells than in a population of filamentous cells in which division was inhibited by inactivation or depletion of FtsZ, FtsA, FtsQ, FtsW, or FtsN [4].
  • With MraY and FtsW deficiencies the decrease of UDP-MurNAc-pentapeptide was accompanied by an increase of the upstream nucleotide precursors and the appearance of UDP-MurNAc-tetrapeptide [5].
 

Analytical, diagnostic and therapeutic context of ECs0093

  • Immunofluorescence microscopy showed that the FtsZ protein can localize to presumptive division sites in strains carrying ftsW(Ts) mutations at the nonpermissive temperature, suggesting that FtsW is unlikely to be specifically required for the localization of FtsZ to the division site [6].
  • Site-directed mutagenesis experiments combined with fluorescence microscopy shed light on the role of Escherichia coli FtsW, a membrane protein belonging to the SEDS family that is involved in peptidoglycan assembly during cell elongation, division, and sporulation [7].
  • Their membrane addressing in E. coli was demonstrated by cell fractionation and was confirmed for FtsW by immunolocalization [8].

References

  1. Interaction between FtsZ and FtsW of Mycobacterium tuberculosis. Datta, P., Dasgupta, A., Bhakta, S., Basu, J. J. Biol. Chem. (2002) [Pubmed]
  2. Topological characterization of the essential Escherichia coli cell division protein FtsW. Lara, B., Ayala, J.A. FEMS Microbiol. Lett. (2002) [Pubmed]
  3. ftsW is an essential cell-division gene in Escherichia coli. Boyle, D.S., Khattar, M.M., Addinall, S.G., Lutkenhaus, J., Donachie, W.D. Mol. Microbiol. (1997) [Pubmed]
  4. Probing the catalytic activity of a cell division-specific transpeptidase in vivo with beta-lactams. Eberhardt, C., Kuerschner, L., Weiss, D.S. J. Bacteriol. (2003) [Pubmed]
  5. Peptidoglycan precursor pools associated with MraY and FtsW deficiencies or antibiotic treatments. Lara, B., Mengin-Lecreulx, D., Ayala, J.A., van Heijenoort, J. FEMS Microbiol. Lett. (2005) [Pubmed]
  6. Two polypeptide products of the Escherichia coli cell division gene ftsW and a possible role for FtsW in FtsZ function. Khattar, M.M., Addinall, S.G., Stedul, K.H., Boyle, D.S., Lutkenhaus, J., Donachie, W.D. J. Bacteriol. (1997) [Pubmed]
  7. Functional analysis of the cell division protein FtsW of Escherichia coli. Pastoret, S., Fraipont, C., den Blaauwen, T., Wolf, B., Aarsman, M.E., Piette, A., Thomas, A., Brasseur, R., Nguyen-Distèche, M. J. Bacteriol. (2004) [Pubmed]
  8. Expression and purification of FtsW and RodA from Streptococcus pneumoniae, two membrane proteins involved in cell division and cell growth, respectively. Noirclerc-Savoye, M., Morlot, C., Gérard, P., Vernet, T., Zapun, A. Protein Expr. Purif. (2003) [Pubmed]
 
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