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| | !align=left |Citation | ||
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'''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 | |||
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| | !align=left |Abstract | ||
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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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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=19255437 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2660739 PMC2660739] | |||
Online version:[http://dx.doi.org/10.1073/pnas.0811780106 10.1073/pnas.0811780106] | |||
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!align=left |Keywords | |||
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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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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
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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Significance
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Useful Materials and Methods
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Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| 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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EcoliWiki Links
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See also
References
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