The function of the DegP (HtrA) protein: Protease versus chaperone.
The DegP (or HtrA) is a highly conserved family of proteins functioning in all living organisms. It was initially identified as a protease functioning in the periplasmic space of the Gram-negative bacterial cells. It was later reported to also exhibit chaperone activity and thus has been designated as a bifunctional protein. However, recent studies demonstrated that in living cells it more likely functions only as a protease with hardly detectable chaperone activities. In this review, I will summarize the evidences clarifying that DegP more likely only functions as a protease rather than as a chaperone in cells. © 2016 IUBMB Life, 68(11):904-907, 2016.
Center for Protein Science, State Key Laboratory of Protein and Plant Gene Studies, School of Life Sciences, Center for History and Philosophy of Science, Peking University, Beijing, China. changzy@pku.edu.cn.
Zengyi
Z
Chang
D004926:Escherichia coli / Q000201:enzymology; D006360:Heat-Shock Proteins / Q000502:physiology*; D033903:Periplasmic Proteins / Q000502:physiology*; D011499:Protein Processing, Post-Translational; D059748:Proteolysis; D012697:Serine Endopeptidases / Q000502:physiology*
D006360:Heat-Shock Proteins; D033903:Periplasmic Proteins; C061682:DegP protease; D012697:Serine Endopeptidases
outer membrane protein biogenesis; periplasmic space; protein quality control