{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["21(20)"],"submitter":["Hasselblatt H"],"pubmed_abstract":["The unfolded protein response of Escherichia coli is triggered by the accumulation of unassembled outer membrane proteins (OMPs) in the cellular envelope. The PDZ-protease DegS recognizes these mislocalized OMPs and initiates a proteolytic cascade that ultimately leads to the sigmaE-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly. The general features of how OMPs activate the protease function of DegS have not yet been systematically addressed. Furthermore, it is unknown how the PDZ domain keeps the protease inactive in the resting state, which is of crucial importance for the functioning of the entire sigmaE stress response. Here we show in atomic detail how DegS is able to integrate the information of distinct stress signals that or"],"journal":["Genes & development"],"pagination":["2659-70"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2000328"],"repository":["biostudies-literature"],"pubmed_title":["Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress."],"pmcid":["PMC2000328"],"pubmed_authors":["Kurzbauer R","Kirk R","Hasselblatt H","Sawa J","Kurt J","Clausen T","Hasenbein S","Ehrmann M","Wilken C","Krojer T"],"additional_accession":[]},"is_claimable":false,"name":"Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress.","description":"The unfolded protein response of Escherichia coli is triggered by the accumulation of unassembled outer membrane proteins (OMPs) in the cellular envelope. The PDZ-protease DegS recognizes these mislocalized OMPs and initiates a proteolytic cascade that ultimately leads to the sigmaE-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly. The general features of how OMPs activate the protease function of DegS have not yet been systematically addressed. Furthermore, it is unknown how the PDZ domain keeps the protease inactive in the resting state, which is of crucial importance for the functioning of the entire sigmaE stress response. Here we show in atomic detail how DegS is able to integrate the information of distinct stress signals that or","dates":{"release":"2007-01-01T00:00:00Z","publication":"2007 Oct","modification":"2025-04-05T08:50:06.315Z","creation":"2019-03-27T00:13:44Z"},"accession":"S-EPMC2000328","cross_references":{"pubmed":["17938245"],"doi":["10.1101/gad.445307"]}}