Bacterial expression of a eukaryotic membrane protein in fusion to various Mistic orthologs.
Hay Dvir,Senyon Choe +1 more
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TLDR
The concept that expression levels of 'Misticated' membrane proteins are related to the independent chaperoning character of Mistic via direct membrane association, rather than related to specific sequence-dependent interaction with the E. coli translocon machinery is supported.About:
This article is published in Protein Expression and Purification.The article was published on 2009-11-01 and is currently open access. It has received 33 citations till now. The article focuses on the topics: Integral membrane protein & Membrane protein.read more
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Recombinant protein expression and purification: A comprehensive review of affinity tags and microbial applications
TL;DR: This review serves as an excellent literature reference for those working on protein fusion tags and provides summaries of well‐characterized purification strategies that have been used to increase product yields and have widespread application in many areas of biotechnology including drug discovery, therapeutics, and pharmacology.
Journal ArticleDOI
Strategies to optimize protein expression in E. coli.
Dana M. Francis,Rebecca Page +1 more
TL;DR: This overview describes variables at each stage of a protein expression experiment that can influence solubility and offers a summary of strategies used to optimize soluble expression in E. coli.
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Heterologous Expression of Membrane Proteins: Choosing the Appropriate Host
Florent Bernaudat,Florent Bernaudat,Annie Frelet-Barrand,Nathalie Pochon,Nathalie Pochon,Sébastien Dementin,Sébastien Dementin,Patrick Hivin,Sylvain Boutigny,Jean-Baptiste Rioux,Jean-Baptiste Rioux,Daniel Salvi,Daphné Seigneurin-Berny,Pierre Richaud,Pierre Richaud,Jacques Joyard,David Pignol,David Pignol,Monique Sabaty,Monique Sabaty,Thierry Desnos,Thierry Desnos,Eva Pebay-Peyroula,Eva Pebay-Peyroula,Elisabeth Darrouzet,Thierry Vernet,Thierry Vernet,Norbert Rolland +27 more
TL;DR: General recommendations are formulated to assist with choosing an appropriate system for heterologous expression of a membrane protein based on observations of protein behaviour in the different hosts and the results highlight certain factors that should be considered when selecting an expression host.
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Bacterial-based membrane protein production
TL;DR: This work has shown that E. coli strains with strongly improved membrane protein production characteristics can be engineered or selected for, and many membrane proteins can be efficiently produced in E. Escherichia coli-based cell-free systems.
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Revolutionizing membrane protein overexpression in bacteria
Susan Schlegel,Mirjam Klepsch,Dimitra Gialama,David Wickström,Dirk Jan Slotboom,Jan-Willem de Gier +5 more
TL;DR: The bacterium Escherichia coli is the most widely used expression host for overexpression trials of membrane proteins, and recent studies have shown that it is feasible to engineer or select for E. coli strains with strongly improved membrane protein overextression characteristics.
References
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Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
Erik Wallin,G. von Heijne +1 more
TL;DR: Detailed statistical analyses of integral membrane proteins of the helix‐bundle class from eubacterial, archaean, and eukaryotic organisms for which genome‐wide sequence data are available suggest that uni‐cellular organisms appear to prefer proteins with 6 and 12 transmembrane segments, whereas Caenorhabditis elegans and Homo sapiens have a slight preference for proteins with seven transmemBRane segments.
Journal ArticleDOI
X-ray structure of a protein-conducting channel
Bert van den Berg,William M. Clemons,Ian Collinson,Yorgo Modis,Enno Hartmann,Stephen C. Harrison,Tom A. Rapoport +6 more
TL;DR: The crystal structure of the Sec61 or SecY complex from Methanococcus jannaschii suggests mechanisms for signal-sequence recognition and for the lateral exit of transmembrane segments of nascent membrane proteins into lipid, and indicates binding sites for partners that provide the driving force for translocation.
Journal ArticleDOI
Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
TL;DR: Structural, genetic and biochemical data show how the channel opens across the membrane, releases hydrophobic segments of membrane proteins laterally into lipid, and maintains the membrane barrier for small molecules.
Journal ArticleDOI
Structure of a complex of the ATPase SecA and the protein-translocation channel.
TL;DR: The crystal structure of SecA bound to the SecY complex, with a maximum resolution of 4.5 ångström (Å), obtained for components from Thermotoga maritima, shows that one copy ofSecA in an intermediate state of ATP hydrolysis is bound to one molecule of theSecY complex.
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Crystal structure of the tetramerization domain of the Shaker potassium channel
TL;DR: Most highly conserved amino acids in the T1 domain of all known potassium channels are found in the core of the protein, indicating a common structural framework for the tetramer assembly.
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