Enhanced itaconic acid production by self-assembly of two biosynthetic enzymes in Escherichia coli

2016 ◽  
Vol 114 (2) ◽  
pp. 457-462 ◽  
Author(s):  
Zhongwei Yang ◽  
Xin Gao ◽  
Hui Xie ◽  
Fengqing Wang ◽  
Yuhong Ren ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Itaconic Acid ◽  
Self Assembly ◽  
Acid Production ◽  
Biosynthetic Enzymes

Whole-cell Immobilization of Engineered Escherichia coli JY001 with Barium-alginate for Itaconic Acid Production

2018 ◽  
Vol 23 (4) ◽  
pp. 442-447 ◽  
Author(s):  
Yu-Mi Moon ◽  
Ranjit Gurav ◽  
Junyoung Kim ◽  
Yun-Gi Hong ◽  
Shashi Kant Bhatia ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Itaconic Acid ◽  
Acid Production ◽  
Cell Immobilization ◽  
Whole Cell ◽  
Engineered Escherichia Coli

Manufacturing Multienzymatic Complex Reactors In Vivo by Self-Assembly To Improve the Biosynthesis of Itaconic Acid in Escherichia coli

2018 ◽  
Vol 7 (5) ◽  
pp. 1244-1250 ◽  
Author(s):  
Zhongwei Yang ◽  
Hongling Wang ◽  
Yuxiao Wang ◽  
Yuhong Ren ◽  
Dongzhi Wei
Keyword(s):  
Escherichia Coli ◽  
Itaconic Acid ◽  
Self Assembly ◽  
Multienzymatic Complex

Model-based metabolic engineering enables high yield itaconic acid production by Escherichia coli

2016 ◽  
Vol 38 ◽  
pp. 29-37 ◽  
Author(s):  
Björn-Johannes Harder ◽  
Katja Bettenbrock ◽  
Steffen Klamt
Keyword(s):  
Escherichia Coli ◽  
Metabolic Engineering ◽  
Itaconic Acid ◽  
Acid Production ◽  
High Yield ◽  
Model Based

scholarly journals Large domain movements upon UvrD dimerization and helicase activation

2017 ◽  
Vol 114 (46) ◽  
pp. 12178-12183 ◽  
Author(s):  
Binh Nguyen ◽  
Yerdos Ordabayev ◽  
Joshua E. Sokoloski ◽  
Elizabeth Weiland ◽  
Timothy M. Lohman
Keyword(s):  
Escherichia Coli ◽  
Single Molecule ◽  
Self Assembly ◽  
Total Internal Reflection ◽  
Dna Helicase ◽  
Conformational State ◽  
Helicase Activity ◽  
Multiple Conformations ◽  
Dna Substrate

Escherichia coli UvrD DNA helicase functions in several DNA repair processes. As a monomer, UvrD can translocate rapidly and processively along ssDNA; however, the monomer is a poor helicase. To unwind duplex DNA in vitro, UvrD needs to be activated either by self-assembly to form a dimer or by interaction with an accessory protein. However, the mechanism of activation is not understood. UvrD can exist in multiple conformations associated with the rotational conformational state of its 2B subdomain, and its helicase activity has been correlated with a closed 2B conformation. Using single-molecule total internal reflection fluorescence microscopy, we examined the rotational conformational states of the 2B subdomain of fluorescently labeled UvrD and their rates of interconversion. We find that the 2B subdomain of the UvrD monomer can rotate between an open and closed conformation as well as two highly populated intermediate states. The binding of a DNA substrate shifts the 2B conformation of a labeled UvrD monomer to a more open state that shows no helicase activity. The binding of a second unlabeled UvrD shifts the 2B conformation of the labeled UvrD to a more closed state resulting in activation of helicase activity. Binding of a monomer of the structurally similar Escherichia coli Rep helicase does not elicit this effect. This indicates that the helicase activity of a UvrD dimer is promoted via direct interactions between UvrD subunits that affect the rotational conformational state of its 2B subdomain.

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