Assemblies of DegP underlie its dual chaperone and protease function

作者：Subrini Orso; Betton Jean Michel^*

来源：FEMS Microbiology Letters, 2009, 296(2): 143-148.

DOI：10.1111/j.1574-6968.2009.01658.x

• periplasm
• stress
• protein degradation
• protein folding
• chaperone

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.

• 出版日期2009-7