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Vol. 16, No. 16, pp. 2156-2168, August 15, 2002
E-dependent extracytoplasmic stress response
1 Department of Biochemistry and Biophysics,
2 Department of Microbiology and Immunology, and
3 Department of Stomatology, University of California at
San Francisco, San Francisco, California 94143, USA; 4 Harvard
Medical School, Department of Microbiology and Molecular Genetics,
Boston, Massachusetts 02115, USA
All cells have stress response pathways that maintain homeostasis in
each cellular compartment. In the Gram-negative bacterium Escherichia coli, the 
E pathway responds to
protein misfolding in the envelope. The stress signal is transduced
across the inner membrane to the cytoplasm via the inner membrane
protein RseA, the anti-sigma factor that inhibits the transcriptional
activity of E. Stress-induced activation of the pathway
requires the regulated proteolysis of RseA. In this report we show that
RseA is degraded by sequential proteolytic events controlled by the
inner membrane-anchored protease DegS and the membrane-embedded
metalloprotease YaeL, an ortholog of mammalian Site-2 protease (S2P).
This is consistent with the mechanism of activation of ATF6, the
mammalian unfolded protein response transcription factor by Site-1
protease and S2P. Thus, mammalian and bacterial cells employ a
conserved proteolytic mechanism to activate membrane-associated
transcription factors that initiate intercompartmental cellular stress
responses.
[Key Words:
DegS; YaeL; regulated intramembrane
proteolysis; E; ATF6; Site-2 protease]
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