Enhancing recombinant Chaetomium thermophilium Formate Dehydrogenase Expression with CRISPR Technology

Author(s):  
Erhan Ar ◽  
Adem Demiroğlu ◽  
Mahmut Selim Yılmaz ◽  
Berin Yılmazer ◽  
Elif Sibel Aslan ◽  
...  
2019 ◽  
Vol 35 (6) ◽  
pp. 21-29
Author(s):  
T.E. Leonova ◽  
T.E. Shustikova ◽  
T.V. Gerasimova ◽  
Т.А. Ivankova ◽  
K.V. Sidorenko Sidorenko ◽  
...  

Thepsefdh_D221Q gene coding for a mutant formate dehydrogenase (PseFDG_D221Q) from Pseudomonas, which catalyzes the formate oxidation with the simultaneous formation of NADPH, has been expressed in the cells of lysine-producing Corynebacterium glutamicum strains. The psefdh_D221Q gene was introduced into С. glutamicum strains as part of an autonomous plasmid or was integrated into the chromosome with simultaneous inactivation of host formate dehydrogenase genes. It was shown that the С. glutamicum strains with NADP+ -dependent formate dehydrogenase have an increased level of L-lysine synthesis in the presence of formate, if their own formate dehydrogenase is inactivated. L-lysine, formate dehydrogenase, NADPH, Corynebacterium glutamicum The work was carried out using the equipment of the Multipurpose Scientific This work was carried out on the equipment of the Multipurpose Scientific Installation of «All-Russian Collection of Industrial Microorganisms», National Bio-Resource Center, NRC «Kurchatov Institute»- GosNIIgenetika. This work was financially supported by the Ministry of Education and Science of Russia (Unique Project Identifier - RFMEFI61017X0011).


2021 ◽  
Vol 407 ◽  
pp. 127065
Author(s):  
Robert D. Franklin ◽  
Joshua A. Whitley ◽  
Adam A. Caparco ◽  
Bettina R. Bommarius ◽  
Julie A. Champion ◽  
...  

Author(s):  
Julia Alvarez-Malmagro ◽  
Ana R. Oliveira ◽  
Cristina Gutiérrez-Sánchez ◽  
Beatriz Villajos ◽  
Inês A.C. Pereira ◽  
...  

Genetics ◽  
1990 ◽  
Vol 125 (4) ◽  
pp. 691-702 ◽  
Author(s):  
B L Berg ◽  
V Stewart

Abstract Formate oxidation coupled to nitrate reduction constitutes a major anaerobic respiratory pathway in Escherichia coli. This respiratory chain consists of formate dehydrogenase-N, quinone, and nitrate reductase. We have isolated a recombinant DNA clone that likely contains the structural genes, fdnGHI, for the three subunits of formate dehydrogenase-N. The fdnGHI clone produced proteins of 110, 32 and 20 kDa which correspond to the subunit sizes of purified formate dehydrogenase-N. Our analysis indicates that fdnGHI is organized as an operon. We mapped the fdn operon to 32 min on the E. coli genetic map, close to the genes for cryptic nitrate reductase (encoded by the narZ operon). Expression of phi(fdnG-lacZ) operon fusions was induced by anaerobiosis and nitrate. This induction required fnr+ and narL+, two regulatory genes whose products are also required for the anaerobic, nitrate-inducible activation of the nitrate reductase structural gene operon, narGHJI. We conclude that regulation of fdnGHI and narGHJI expression is mediated through common pathways.


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