FtsZ-dependent localization of GroEL protein at possible division sites.
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.
Department of Bioengineering, Tokyo Institute of Technology, 4259-B-38 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
Hidetaka
H
Ogino
Masaaki
M
Wachi
Akihiro
A
Ishii
Noritaka
N
Iwai
Tetsuya
T
Nishida
Sakuo
S
Yamada
Kazuo
K
Nagai
Motoyuki
M
Sugai
D002455:Cell Division; D018834:Chaperonin 60 / Q000032:analysis* / Q000502:physiology; D022162:Cytoplasmic Vesicles / Q000737:chemistry / Q000648:ultrastructure; D004926:Escherichia coli / Q000737:chemistry / Q000166:cytology* / Q000648:ultrastructure; D029968:Escherichia coli Proteins / Q000502:physiology*; D008856:Microscopy, Fluorescence; D010406:Penicillins / Q000494:pharmacology
D018834:Chaperonin 60; D029968:Escherichia coli Proteins; C076835:FtsZ84 protein, E coli; D010406:Penicillins