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Journal of Bacteriology, November 2008, p. 7117-7122, Vol. 190, No. 21
0021-9193/08/$08.00+0     doi:10.1128/JB.00871-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Dual Role of FtsH in Regulating Lipopolysaccharide Biosynthesis in Escherichia coli{triangledown}

Chen Katz and Eliora Z. Ron*

Department of Molecular Microbiology and Biotechnology, Life Sciences, Tel Aviv University, Tel Aviv, Israel 69978

Received 25 June 2008/ Accepted 26 August 2008

In Escherichia coli, FtsH (HflB) is a membrane-bound, ATP-dependent metalloendoprotease belonging to the AAA family (ATPases associated with diverse cellular activities). FtsH has a limited spectrum of known substrates, including the transcriptional activator {sigma}32. FtsH is the only known E. coli protease that is essential, as it regulates the concentration of LpxC, which carries out the first committed step in the synthesis of lipid A. Here we identify a new FtsH substrate—3-deoxy-D-manno-octulosonate (KDO) transferase—which carries out the attachment of two KDO residues to the lipid A precursor (lipid IVA) to form the minimal essential structure of the lipopolysaccharide (LPS) (KDO2-lipid A). Thus, FtsH regulates the concentration of the lipid moiety of LPS (lipid A) as well as the sugar moiety (KDO-based core oligosaccharides), ensuring a balanced synthesis of LPS.


* Corresponding author. Mailing address: Department of Molecular Microbiology and Biotechnology, Life Sciences, Tel Aviv University, Tel Aviv, Israel 69978. Phone: 972-3-6409379. Fax: 972-3-6414138. E-mail: eliora{at}post.tau.ac.il

{triangledown} Published ahead of print on 5 September 2008.


Journal of Bacteriology, November 2008, p. 7117-7122, Vol. 190, No. 21
0021-9193/08/$08.00+0     doi:10.1128/JB.00871-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.




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