Assemblies of DegP underlie its dual chaperone and protease function.
Molecular chaperones and energy-dependent proteases are essential components of cellular protein quality control. Many of these proteins form heterocomplexes that promote either refolding or degradation of misfolded proteins. Recent structural studies showed how DegP, a periplasmic heat-shock protease of Escherichia coli, assembles into large homooligomers with an internal cavity combining both chaperone and protease activity.
Subrini
Orso
O
Unité Biochimie Structurale, CNRS URA2185, Institut Pasteur, Paris, France.
Betton
Jean-Michel
JM
D004926:Escherichia coli / Q000201:enzymology*; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000502:physiology*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000502:physiology*; D033903:Periplasmic Proteins / Q000737:chemistry / Q000502:physiology*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D012697:Serine Endopeptidases / Q000737:chemistry / Q000502:physiology*
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D033903:Periplasmic Proteins; C061682:DegP protease; D012697:Serine Endopeptidases