title: A PDZ switch for a cellular stress response.
abstract: The accumulation of misfolded porins in the periplasm of bacteria triggers a proteolytic cascade, initiated by activation of DegS, a member of the family of HtrA proteases. Activation of DegS ultimately leads to the expression of genes encoding the periplasmic protein folding machinery. A new study now reveals that binding of exposed C-termini of unassembled porins to the PDZ domain of DegS induces structural rearrangements that activate the catalytic site of the protease domain.
authors.affiliation: Zentrum für Molekulare Biologie Heidelberg, Universität Heidelberg, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.
authors.forename: Christian
authors.initials: C
authors.lastname: Schlieker
authors.forename: Axel
authors.initials: A
authors.lastname: Mogk
authors.forename: Bernd
authors.initials: B
authors.lastname: Bukau
mesh_terms: D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D020134:Catalytic Domain / Q000502:physiology; D018272:Porins / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D017510:Protein Folding
chemical_list: D001426:Bacterial Proteins; C066496:DegS protein, Bacteria; D018272:Porins