The genes for the eight subunits of the membrane bound ATP synthase of Escherichia coli

1981 ◽  
Vol 183 (3) ◽  
pp. 463-472 ◽  
Author(s):  
Flemming G. Hansen ◽  
Jørgen Nielsen ◽  
Erik Riise ◽  
Kaspar von Meyenburg
1984 ◽  
Vol 3 (8) ◽  
pp. 1791-1797 ◽  
Author(s):  
K. von Meyenburg ◽  
B.B. Jørgensen ◽  
B. van Deurs

1981 ◽  
Vol 184 (1) ◽  
pp. 33-39 ◽  
Author(s):  
Jørgen Nielsen ◽  
Flemming G. Hansen ◽  
Jürgen Hoppe ◽  
Peter Friedl ◽  
Kaspar von Meyenburg

1985 ◽  
Vol 4 (9) ◽  
pp. 2357-2363 ◽  
Author(s):  
K. von Meyenburg ◽  
B.B. Jørgensen ◽  
O. Michelsen ◽  
L. Sørensen ◽  
J.E. McCarthy

1982 ◽  
Vol 188 (2) ◽  
pp. 240-248 ◽  
Author(s):  
Kaspar von Meyenburg ◽  
Birgitte Bojer Jørgensen ◽  
Jørgen Nielsen ◽  
Flemming G. Hansen

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Jasmine M. Hershewe ◽  
Katherine F. Warfel ◽  
Shaelyn M. Iyer ◽  
Justin A. Peruzzi ◽  
Claretta J. Sullivan ◽  
...  

AbstractCell-free gene expression (CFE) systems from crude cellular extracts have attracted much attention for biomanufacturing and synthetic biology. However, activating membrane-dependent functionality of cell-derived vesicles in bacterial CFE systems has been limited. Here, we address this limitation by characterizing native membrane vesicles in Escherichia coli-based CFE extracts and describing methods to enrich vesicles with heterologous, membrane-bound machinery. As a model, we focus on bacterial glycoengineering. We first use multiple, orthogonal techniques to characterize vesicles and show how extract processing methods can be used to increase concentrations of membrane vesicles in CFE systems. Then, we show that extracts enriched in vesicle number also display enhanced concentrations of heterologous membrane protein cargo. Finally, we apply our methods to enrich membrane-bound oligosaccharyltransferases and lipid-linked oligosaccharides for improving cell-free N-linked and O-linked glycoprotein synthesis. We anticipate that these methods will facilitate on-demand glycoprotein production and enable new CFE systems with membrane-associated activities.


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