Escherichia coli as host for membrane protein structure determination: a global analysis

Hattab G, Warschawski DE, Moncoq K, Miroux B (2015)
Scientific Reports 5: 12097.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
The structural biology of membrane proteins (MP) is hampered by the difficulty in producing and purifying them. A comprehensive analysis of protein databases revealed that 213 unique membrane protein structures have been obtained after production of the target protein in E. coli. The primary expression system used was the one based on the T7 RNA polymerase, followed by the arabinose and T5 promoter based expression systems. The C41λ(DE3) and C43λ(DE3) bacterial mutant hosts have contributed to 28% of non E. coli membrane protein structures. A large scale analysis of expression protocols demonstrated a preference for a combination of bacterial host-vector together with a bimodal distribution of induction temperature and of inducer concentration. Altogether our analysis provides a set of rules for the optimal use of bacterial expression systems in membrane protein production.
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Scientific Reports
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5
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12097
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Hattab G, Warschawski DE, Moncoq K, Miroux B. Escherichia coli as host for membrane protein structure determination: a global analysis. Scientific Reports. 2015;5:12097.
Hattab, G., Warschawski, D. E., Moncoq, K., & Miroux, B. (2015). Escherichia coli as host for membrane protein structure determination: a global analysis. Scientific Reports, 5, 12097. doi:10.1038/srep12097
Hattab, G., Warschawski, D. E., Moncoq, K., and Miroux, B. (2015). Escherichia coli as host for membrane protein structure determination: a global analysis. Scientific Reports 5, 12097.
Hattab, G., et al., 2015. Escherichia coli as host for membrane protein structure determination: a global analysis. Scientific Reports, 5, p 12097.
G. Hattab, et al., “Escherichia coli as host for membrane protein structure determination: a global analysis”, Scientific Reports, vol. 5, 2015, pp. 12097.
Hattab, G., Warschawski, D.E., Moncoq, K., Miroux, B.: Escherichia coli as host for membrane protein structure determination: a global analysis. Scientific Reports. 5, 12097 (2015).
Hattab, Georges, Warschawski, Dror E., Moncoq, Karine, and Miroux, Bruno. “Escherichia coli as host for membrane protein structure determination: a global analysis”. Scientific Reports 5 (2015): 12097.

4 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Isolation and characterization of the E. coli membrane protein production strain Mutant56(DE3).
Baumgarten T, Schlegel S, Wagner S, Löw M, Eriksson J, Bonde I, Herrgård MJ, Heipieper HJ, Nørholm MH, Slotboom DJ, de Gier JW., Sci Rep 7(), 2017
PMID: 28338018
Double promoter expression systems for recombinant protein production by industrial microorganisms.
Öztürk S, Ergün BG, Çalık P., Appl Microbiol Biotechnol 101(20), 2017
PMID: 28900685
Current strategies for protein production and purification enabling membrane protein structural biology.
Pandey A, Shin K, Patterson RE, Liu XQ, Rainey JK., Biochem Cell Biol 94(6), 2016
PMID: 27010607

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Daten bereitgestellt von Europe PubMed Central.

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