PMID:19255437

Shen, QT, Bai, XC, Chang, LF, Wu, Y, Wang, HW and Sui, SF (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

<protect>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.

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Online version:10.1073/pnas.0811780106 |} </protect>

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Annotations

Gene product	Qualifier	GO ID	GO term name	Evidence Code	with/from	Aspect	Notes	Status
degP:Gene_Product(s)		GO:0004252	serine-type endopeptidase activity	IMP: Inferred from Mutant Phenotype		F	Proteolytic activity of purified wild-type and several deletion mutants was assayed using beta-casein as the substrate and shown to be reduced in the mutants (Figure 4E).	complete
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