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Journal of Bacteriology, July 2005, p. 4552-4561, Vol. 187, No. 13
0021-9193/05/$08.00+0     doi:10.1128/JB.187.13.4552-4561.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Characterization of Six Lipoproteins in the ^E Regulon

Department of Biochemistry & Biophysics, University of California, San Francisco, California 94143,¹ Departments of Microbiology and Laboratory Medicine, University of Washington, Seattle, Washington 98195,² Departments of Stomatology and Microbiology & Immunology, University of California, San Francisco, California 94143-2200³

Received 22 December 2004/ Accepted 24 March 2005

In Escherichia coli, ^E regulon functions are required for envelope homeostasis during stress and are essential for viability under all growth conditions. The E. coli genome encodes approximately 100 lipoproteins, and 6 of these are regulated by ^E. Phenotypes associated with deletion of each of these lipoproteins are the subject of this report. One lipoprotein, YfiO, is essential for cellular viability. However, overexpression of this protein is not sufficient to alleviate the requirement of ^E for viability, suggesting that the ^E regulon provides more than one essential function. The remaining five lipoproteins in the ^E regulon are nonessential; cells are viable even when all five are removed simultaneously. Deletion of three nonessential lipoprotein genes (nlpB, yraP, ygfL) results in the exhibition of phenotypes that suggest they are important for maintenance of the integrity of the cell envelope. nlpB cells are selectively sensitive to rifampin; yraP cells are selectively sensitive to sodium dodecyl sulfate. Such selective sensitivity has not been previously reported. Both yraP and nlpB are synthetically lethal with surA::Cm, which encodes a periplasmic chaperone and PPIase, suggesting that NlpB and YraP play roles in a periplasmic folding pathway that functions in parallel with that of SurA. Finally, the yfgL mutant exhibits a broad range of envelope defects, including sensitivity to several membrane-impermeable agents, an altered outer membrane protein profile, synthetic lethality with both surA::Cm and fkpA::Cm strains, and sensitivity to a bactericidal permeability-increasing peptide. We suggest that this lipoprotein performs a very important but as-yet-unknown function in maintaining the integrity of the cell envelope.

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