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Microbial Cell Factories

, 8:69

First Online: 29 December 2009Received: 15 October 2009Accepted: 29 December 2009

Abstract

The last four years have brought exciting progress in membrane protein research. Finally those many efforts that have been put into expression of eukaryotic membrane proteins are coming to fruition and enable to solve an ever-growing number of high resolution structures. In the past, many skilful optimization steps were required to achieve sufficient expression of functional membrane proteins. Optimization was performed individually for every membrane protein, but provided insight about commonly encountered bottlenecks and, more importantly, general guidelines how to alleviate cellular limitations during microbial membrane protein expression. Lately, system-wide analyses are emerging as powerful means to decipher cellular bottlenecks during heterologous protein production and their use in microbial membrane protein expression has grown in popularity during the past months.

This review covers the most prominent solutions and pitfalls in expression of eukaryotic membrane proteins using microbial hosts prokaryotes, yeasts, highlights skilful applications of our basic understanding to improve membrane protein production. Omics technologies provide new concepts to engineer microbial hosts for membrane protein production.

List of Abbreviations usedCYPcytochrome P450

DMSOdimethyl sulfoxide

ERendoplasmic reticulum

FACSFluorescence Activated Cell Sorting

GAL1galactose kinase

GAL10UDP-glucose 4-epimerase

GFPgreen fluorescent protein

GPCRG protein coupled receptor

HTPhigh throughput

IMPintegral membrane protein

NMRnuclear magnetic resonance

PTMposttranslational modification

SRPsignal recognition particle

TMHtransmembrane helix

UPRunfolded protein response.

Electronic supplementary materialThe online version of this article doi:10.1186-1475-2859-8-69 contains supplementary material, which is available to authorized users.

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Autor: Maria Freigassner - Harald Pichler - Anton Glieder

Fuente: https://link.springer.com/



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