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Journal ArticleDOI

Preparative expression of secreted proteins in bacteria : status report and future prospects

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TLDR
The expression of heterologous secreted proteins in Escherichia coli is widely employed for laboratory and preparative purposes and protein design and directed evolution approaches are beginning to be exploited for engineering of the cellular protein folding machinery to achieve further improvements in protein expression.
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This article is published in Current Opinion in Biotechnology.The article was published on 2005-10-01. It has received 222 citations till now. The article focuses on the topics: Periplasmic space & Protein design.

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Journal ArticleDOI

Recombinant protein expression in Escherichia coli: advances and challenges.

TL;DR: The different approaches for the synthesis of recombinant proteins in E. coli are reviewed and recent progress in this ever-growing field is discussed.
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Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems.

TL;DR: An overview of the most commonly used promoter systems for recombinant proteins, including Bacillus brevis, Bacillusmegaterium, Bacillussubtilis, Caulobacter crescentus, other strains, and, most importantly, Escherichia coli BL21 and E. coli K12 and their derivatives are presented.
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Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes.

TL;DR: The most frequently used prokaryotic, yeast, insect and mammalian expression systems, as well as expression in eukaryote individuals are reviewed and the merits and demerits of these systems are discussed.
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The bacterial twin-arginine translocation pathway.

TL;DR: The twin-arginine translocation (Tat) pathway is responsible for the export of folded proteins across the cytoplasmic membrane of bacteria and holds promise for biotechnological applications.
References
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Journal ArticleDOI

Molecular Basis of Bacterial Outer Membrane Permeability Revisited

TL;DR: This review summarizes the development in the field since the previous review and begins to understand how this bilayer of the outer membrane can retard the entry of lipophilic compounds, owing to increasing knowledge about the chemistry of lipopolysaccharide from diverse organisms and the way in which lipopoly Saccharide structure is modified by environmental conditions.
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Recombinant protein folding and misfolding in Escherichia coli.

TL;DR: The past 20 years have seen enormous progress in the understanding of the mechanisms used by the enteric bacterium Escherichia coli to promote protein folding, support protein translocation and handle protein misfolding, and these insights have been exploited to tackle the problems of inclusion body formation, proteolytic degradation and disulfide bond generation.
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A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.

TL;DR: It is shown here that the widely conserved heat shock protein DegP (HtrA) has both general molecular chaperone and proteolytic activities, which mean that a single cellular factor can switch between two key pathways, controlling protein stability and turnover.
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Identification of a Multicomponent Complex Required for Outer Membrane Biogenesis in Escherichia coli

TL;DR: Genetic interactions suggest a role for YfgL, one of the lipoprotein components of the protein assembly complex, in a homeostatic control mechanism that coordinates the overall OM assembly process.
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Secretory and extracellular production of recombinant proteins using Escherichia coli

TL;DR: Recent advances in secretory and extracellular production of recombinant proteins using E. coli are discussed, including the twin-arginine translocation system, which has recently been employed for the efficient secretion of folded proteins.
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