Pinus taeda phenylpropenal double-bond reductase: Purification, cDNA cloning, heterologous expression in Escherichia coli, and subcellular localization in P. taeda☆

2006 ◽  
Vol 67 (16) ◽  
pp. 1765-1780 ◽  
Author(s):  
Hiroyuki Kasahara ◽  
Ying Jiao ◽  
Diana L. Bedgar ◽  
Sung-Jin Kim ◽  
Ann M. Patten ◽  
...  
2008 ◽  
Vol 78 (6) ◽  
pp. 973-981 ◽  
Author(s):  
Zhizhuang Xiao ◽  
Jason Boyd ◽  
Stephan Grosse ◽  
Manon Beauchemin ◽  
Elizabeth Coupe ◽  
...  

2011 ◽  
Vol 92 (4) ◽  
pp. 769-777 ◽  
Author(s):  
José Miguel Araya-Garay ◽  
Lucía Feijoo-Siota ◽  
Patricia Veiga-Crespo ◽  
Tomás González Villa

2012 ◽  
Vol 40 (6) ◽  
pp. 1222-1226 ◽  
Author(s):  
Katrin Richter ◽  
Johannes Gescher

Heterologous multiprotein expression is the tool to answer a number of questions in basic science as well as to convert strains into producers and/or consumers of certain compounds in applied sciences. Multiprotein expression can be driven by plasmids with the disadvantages that the gene dosage might, in some cases, lead to toxic effects and that the continuous addition of antibiotics is undesirable. Stable genomic expression of proteins can forgo these problems and is a helpful and promising tool in synthetic biology. In the present paper, we provide an extract of methods from the toolbox for chromosome-based heterologous expression in Escherichia coli.


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