Literature DB >> 3539017

Localization of inclusion bodies in Escherichia coli overproducing beta-lactamase or alkaline phosphatase.

G Georgiou, J N Telford, M L Shuler, D B Wilson.   

Abstract

High-level synthesis of the periplasmic protein beta-lactamase in Escherichia coli caused the formation of insoluble protein precipitates called inclusion bodies. beta-Lactamase inclusion bodies differed from those reported previously in that they appeared to be localized in the periplasmic space, not in the cytoplasm. The inclusion bodies contained mature beta-lactamase and were solubilized more easily than has been reported for cytoplasmic inclusion bodies. In contrast, overproduction of the periplasmic protein alkaline phosphatase caused the formation of cytoplasmic inclusion bodies containing alkaline phosphatase precursor.

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Year:  1986        PMID： 3539017      PMCID： PMC239190          DOI： 10.1128/aem.52.5.1157-1161.1986

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN： 0099-2240            Impact factor:   4.792


  12 in total

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Review 5.  Genetic analysis of protein export in Escherichia coli K12.

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Authors:  H Inouye; S Michaelis; A Wright; J Beckwith
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9.  Precursor of beta-lactamase is enzymatically inactive. Accumulation of the preprotein in Saccharomyces cerevisiae.

Authors:  R Roggenkamp; H Dargatz; C P Hollenberg
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10.  Cytoplasmic inclusion bodies in Escherichia coli producing biosynthetic human insulin proteins.

Authors:  D C Williams; R M Van Frank; W L Muth; J P Burnett
Journal:  Science       Date:  1982-02-05       Impact factor: 47.728
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  19 in total

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5.  Cosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins.

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6.  Type II secretion by Aeromonas salmonicida: evidence for two periplasmic pools of proaerolysin.

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7.  Folding and aggregation of TEM beta-lactamase: analogies with the formation of inclusion bodies in Escherichia coli.

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8.  Size characterization of inclusion bodies by sedimentation field-flow fractionation.

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9.  Periplasmic aggregation limits the proteolytic maturation of the Escherichia coli penicillin G amidase precursor polypeptide.

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10.  Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.

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