Difference between revisions of "PMID:3278319"

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'''Strauch, KL and Beckwith, J'''  (1988) An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. ''Proc. Natl. Acad. Sci. U.S.A.'' '''85''':1576-80
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!align=left align='left' bgcolor='#CCCCFF' |Abstract
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A fusion between tsr (encoding the inner membrane protein Tsr) and phoA (encoding the periplasmic protein alkaline phosphatase, AP) generates a membrane-bound hybrid protein (Tsr-AP 2) with AP enzymatic activity. The hybrid protein is proteolytically unstable and is broken down to yield a smaller, soluble species with AP activity. We devised a genetic screen to distinguish between cells containing only membrane-bound AP and those containing soluble AP. The screen depends on diffusion of soluble AP away from cells with a leaky outer membrane to produce a halo of AP activity around colonies on solid growth medium. Several mutants lacking this halo show reduced degradation of Tsr-AP 2. One mutant is also defective in breakdown of five other abnormal periplasmic proteins but not of two cytoplasmic proteins. The mutation in this strain, degP4::Tn5, defines a locus distinct from previously identified loci that affect protein stability or protease activities. This strain may be useful for preventing the breakdown of unstable foreign proteins in Escherichia coli.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3278319 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC279816 PMC279816]
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Alkaline Phosphatase/metabolism; Bacterial Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Membrane Proteins/metabolism; Molecular Weight; Mutation; Peptide Hydrolases/genetics; Peptide Hydrolases/metabolism; Recombinant Fusion Proteins/metabolism; Recombinant Proteins/metabolism
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==Main Points of the Paper ==
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== Materials and Methods Used ==
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==Phenotype Annotations==
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==Notes==
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==References==
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[[Category:Publication]]

Latest revision as of 07:37, 5 March 2019

Citation

Strauch, KL and Beckwith, J (1988) An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins. Proc. Natl. Acad. Sci. U.S.A. 85:1576-80

Abstract

A fusion between tsr (encoding the inner membrane protein Tsr) and phoA (encoding the periplasmic protein alkaline phosphatase, AP) generates a membrane-bound hybrid protein (Tsr-AP 2) with AP enzymatic activity. The hybrid protein is proteolytically unstable and is broken down to yield a smaller, soluble species with AP activity. We devised a genetic screen to distinguish between cells containing only membrane-bound AP and those containing soluble AP. The screen depends on diffusion of soluble AP away from cells with a leaky outer membrane to produce a halo of AP activity around colonies on solid growth medium. Several mutants lacking this halo show reduced degradation of Tsr-AP 2. One mutant is also defective in breakdown of five other abnormal periplasmic proteins but not of two cytoplasmic proteins. The mutation in this strain, degP4::Tn5, defines a locus distinct from previously identified loci that affect protein stability or protease activities. This strain may be useful for preventing the breakdown of unstable foreign proteins in Escherichia coli.

Links

PubMed PMC279816

Keywords

Alkaline Phosphatase/metabolism; Bacterial Proteins/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Membrane Proteins/metabolism; Molecular Weight; Mutation; Peptide Hydrolases/genetics; Peptide Hydrolases/metabolism; Recombinant Fusion Proteins/metabolism; Recombinant Proteins/metabolism

Main Points of the Paper

Please summarize the main points of the paper.

Materials and Methods Used

Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).

Phenotype Annotations

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Phenotype of Taxon Information Genotype Information (if known) Condition Information OMP ID OMP Term Name ECO ID ECO Term Name Notes Status

Notes

References

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