FtsZ-dependent localization of GroEL protein at possible division sites

Genes Cells. 2004 Sep;9(9):765-71. doi: 10.1111/j.1365-2443.2004.00770.x.


When Escherichia coli is treated with penicillin, the envelopes bulge at the centre of the cells and the cells then lyse. The bulges expand into vesicle-like structures termed penicillin-induced vesicles. We have developed a method to isolate these structures and have shown that they contain mainly membrane proteins plus a high concentration of a 60 kDa protein. The N-terminal amino acid sequence of the protein is identical to that of GroEL protein. Western blotting analysis using anti-GroEL antibody showed that GroEL is indeed concentrated in the vesicles. Indirect immuno-fluorescence microscopy showed that GroEL protein is localized at the centre of the cells at the site of formation of FtsZ-rings. Localization of GroEL is dependent on FtsZ but not other Fts proteins. GroEL mutants formed elongated cells having no or asymmetrically localized FtsZ-rings at the restrictive temperature. These findings suggest a possible role of the GroEL protein in cell division.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Division
  • Chaperonin 60 / analysis*
  • Chaperonin 60 / physiology
  • Cytoplasmic Vesicles / chemistry
  • Cytoplasmic Vesicles / ultrastructure
  • Escherichia coli / chemistry
  • Escherichia coli / cytology*
  • Escherichia coli / ultrastructure
  • Escherichia coli Proteins / physiology*
  • Microscopy, Fluorescence
  • Penicillins / pharmacology


  • Chaperonin 60
  • Escherichia coli Proteins
  • FtsZ84 protein, E coli
  • Penicillins