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Journal of Bacteriology, August 2007, p. 5860-5866, Vol. 189, No. 16
0021-9193/07/$08.00+0     doi:10.1128/JB.00493-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Filamentous Morphology in GroE-Depleted Escherichia coli Induced by Impaired Folding of FtsE{triangledown}

Kei Fujiwara and Hideki Taguchi*

Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, FSB-401, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8562, Japan

Received 31 March 2007/ Accepted 25 May 2007

The chaperonin GroE (GroEL and the cochaperonin GroES) is the only chaperone system that is essential for the viability of Escherichia coli. It is known that GroE-depleted cells exhibit a filamentous morphology, suggesting that GroE is required for the folding of proteins involved in cell division. Although previous studies, including proteome-wide analyses of GroE substrates, have suggested several targets of GroE in cell division, there is no direct in vivo evidence to identify which substrates exhibit obligate dependence on GroE for folding. Among the candidate substrates, we found that prior excess production of FtsE, a protein engaged in cell division, completely suppressed the filamentation of GroE-depleted E. coli. The GroE depletion led to a drastic decrease in FtsE, and the cells exhibited a known phenotype associated with impaired FtsE function. In the GroE-depleted filamentous cells, the localizations of FtsA and ZipA, both of which assemble with the FtsZ septal ring before FtsE, were normal, whereas FtsX, the interaction partner of FtsE, and FtsQ, which is recruited after FtsE, did not localize to the ring, suggesting that the decrease in FtsE is a cause of the filamentous morphology. Finally, a reconstituted cell-free translation system revealed that the folding of newly translated FtsE was stringently dependent on GroEL/GroES. Based on these findings, we concluded that FtsE is a target substrate of the GroE system in E. coli cell division.

* Corresponding author. Mailing address: Department of Medical Genome Sciences, Graduate School of Frontier Sciences, The University of Tokyo, FSB-401, 5-1-5 Kashiwanoha, Kashiwa, Chiba 277-8562, Japan. Phone and fax: 81 4 7136 3644. E-mail: taguchi{at}k.u-tokyo.ac.jp

{triangledown} Published ahead of print on 8 June 2007.

Journal of Bacteriology, August 2007, p. 5860-5866, Vol. 189, No. 16
0021-9193/07/$08.00+0     doi:10.1128/JB.00493-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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  • Koike-Takeshita, A., Yoshida, M., Taguchi, H. (2008). Revisiting the GroEL-GroES Reaction Cycle via the Symmetric Intermediate Implied by Novel Aspects of the GroEL(D398A) Mutant. J. Biol. Chem. 283: 23774-23781 [Abstract] [Full Text]  
  • Samaluru, H., SaiSree, L., Reddy, M. (2007). Role of SufI (FtsP) in Cell Division of Escherichia coli: Evidence for Its Involvement in Stabilizing the Assembly of the Divisome. J. Bacteriol. 189: 8044-8052 [Abstract] [Full Text]  


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