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Genes to Cells (2004) 9, 765-771. doi:10.1111/j.1365-2443.2004.00770.x
© 2004 Blackwell Publishing or its licensors

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FtsZ-dependent localization of GroEL protein at possible division sites

Hidetaka Ogino1, Masaaki Wachi1,*, Akihiro Ishii1, Noritaka Iwai1, Tetsuya Nishida2, Sakuo Yamada3, Kazuo Nagai4 and Motoyuki Sugai2

1 Department of Bioengineering, Tokyo Institute of Technology, 4259-B-38 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan
2 Department of Bacteriology, Hiroshima University Graduate School of Biomedical Sciences, Kasumi 1-2-3, Minami-ku, Hiroshima 734-8553, Japan
3 Department of Microbiology, Kawasaki Medical School, 577 Matsushima, Kurashiki, Okayama 701-0192, Japan
4 Department of Biological Chemistry, Chubu University, 1200 Matsumoto-cho, Kasugai, Aichi 487-8501, Japan

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.


Communicated by: Hiroji Aiba

* Correspondence: E-mail: mwachi{at}bio.titech.ac.jp




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