PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease.
DegP (HtrA) is a periplasmic heat shock serine protease of Escherichia coli that degrades misfolded proteins at high temperatures. Biochemical and biophysical experiments have indicated that the purified DegP exists as a hexamer. To examine whether the PDZ domains of DegP were required for oligomerization, we constructed a DegP variant lacking both PDZ domains. This truncated variant, DegPDelta, exhibited no proteolytic activity but exerted a dominant-negative effect on growth at high temperatures by interfering with the functional assembly of oligomeric DegP. Thus, the PDZ domains contain information necessary for proper assembly of the functional hexameric structure of DegP.
Unité de Programmation Moléculaire et de Toxicologie Génétique/CNRS-URA1444, Département des Biotechnologies, Institut Pasteur, 25, rue du Docteur Roux, 75015 Paris, France.
N
N
Sassoon
J P
JP
Arié
J M
JM
Betton
D001426:Bacterial Proteins / Q000737:chemistry*; D002455:Cell Division; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006360:Heat-Shock Proteins; D013058:Mass Spectrometry; D009154:Mutation; D033903:Periplasmic Proteins; D011487:Protein Conformation; D017510:Protein Folding; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000235:genetics; D013104:Spheroplasts / Q000201:enzymology; D013696:Temperature
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D033903:Periplasmic Proteins; C061682:DegP protease; D012697:Serine Endopeptidases