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Journal of Bacteriology, January 2003, p. 148-154, Vol. 185, No. 1
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.1.148-154.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Protease-Deficient DegP Suppresses Lethal Effects of a Mutant OmpC Protein by Its Capture

Maria CastilloKeller1 and Rajeev Misra1,2*

Molecular and Cellular Biology Program,1 Department of Microbiology, Arizona State University, Tempe, Arizona 85287-27012

Received 1 August 2002/ Accepted 7 October 2002

The expression of assembly-defective outer membrane proteins can confer lethality if they are not degraded by envelope proteases. We report here that the expression of a mutant OmpC protein, OmpC2Cys, which forms disulfide bonds in the periplasm due to the presence of two non-native cysteine residues, is lethal in cells lacking the major periplasmic protease, DegP. This lethality is not observed in dsbA strains that have diminished ability to form periplasmic disulfide bonds. Our data show that this OmpC2Cys-mediated lethality in a degP::Kmr dsbA+ background can be reversed by a DegP variant, DegPS210A, that is devoid of its proteolytic activity but retains its reported chaperone activity. However, DegPS210A does not reverse the lethal effect of OmpC2Cys by correcting its assembly but rather by capturing misfolded mutant OmpC polypeptides and thus removing them from the assembly pathway. Displacement of OmpC2Cys by DegPS210A also alleviates the negative effect that the mutant OmpC protein has on wild-type OmpF.

* Corresponding author. Mailing address: Molecular and Cellular Biology Program, Arizona State University, Tempe, AZ 85287-2701. Phone: (480) 965-3320. Fax: (480) 965-0098. E-mail: rajeev.misra{at}asu.edu.

Journal of Bacteriology, January 2003, p. 148-154, Vol. 185, No. 1
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.1.148-154.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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