DegS and YaeL participate sequentially in the cleavage of RseA to activate the ς<sup>E</sup>-dependent extracytoplasmic stress response

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<jats:p>All cells have stress response pathways that maintain homeostasis in each cellular compartment. In the Gram-negative bacterium<jats:italic>Escherichia coli,</jats:italic> the ς<jats:sup>E</jats:sup> 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 ς<jats:sup>E</jats:sup>. 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.</jats:p>

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  • Genes & Development

    Genes & Development 16 (16), 2156-2168, 2002-08-15

    Cold Spring Harbor Laboratory

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