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Revision as of 19:06, 1 September 2013
| Citation |
No author listed (2009) Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control. Proc. Natl. Acad. Sci. U.S.A. 106:4858-63 |
|---|---|
| Abstract |
In the periplasm of Escherichia coli, DegP (also known as HtrA), which has both chaperone-like and proteolytic activities, prevents the accumulation of toxic misfolded and unfolded polypeptides. In solution, upon binding to denatured proteins, DegP forms large cage-like structures. Here, we show that DegP forms a range of bowl-shaped structures, independent of substrate proteins, each with a 4-, 5-, or 6-fold symmetry and all with a DegP trimer as the structural unit, on lipid membranes. These membrane-bound DegP assemblies have the capacity to recruit and process substrates in the bowl chamber, and they exhibit higher proteolytic and lower chaperone-like activities than DegP in solution. Our findings imply that DegP might regulate its dual roles during protein quality control, depending on its assembly state in the narrow bacterial envelope. |
| Links |
PubMed PMC2660739 Online version:10.1073/pnas.0811780106 |
| Keywords |
Cell Membrane/enzymology; Cell Membrane/ultrastructure; Escherichia coli/cytology; Escherichia coli/enzymology; Escherichia coli/ultrastructure; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/ultrastructure; Lipids/chemistry; Molecular Chaperones/metabolism; Periplasmic Proteins/chemistry; Periplasmic Proteins/ultrastructure; Protein Processing, Post-Translational; Protein Structure, Quaternary; Serine Endopeptidases/chemistry; Serine Endopeptidases/ultrastructure; Substrate Specificity |
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