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. 2019 Sep 4;9:313. doi: 10.3389/fcimb.2019.00313

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Copyright © 2019 Hews, Cho, Rowley and Raivio.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Regulated intramembrane proteolysis (RIP) leads to activation of the σ^E ESR. In the presence of misfolded proteins, a conformational change as a result of misfolded proteins binding to the PDZ domain of DegS occurs. Subsequently the protease domain of DegS is exposed and the periplasmic domain of RseA is cleaved. RseP then cleaves RseA at the cytoplasmic domain, releasing the σ^E-bound RseA portion into the cytoplasm. Binding of the adaptor protein SspB to RseA-σ^E recruits the ClpXP protease for degradation of RseA and release of free σ^E. σ^E binds to RNA polymerase and transcription of the σ^E regulon is induced.