Faculty Opinions recommendation of Selenite assimilation into formate dehydrogenase H depends on thioredoxin reductase in Escherichia coli.

Author(s):  
Russ Hille
2007 ◽  
Vol 143 (4) ◽  
pp. 467-473 ◽  
Author(s):  
M. Takahata ◽  
T. Tamura ◽  
K. Abe ◽  
H. Mihara ◽  
S. Kurokawa ◽  
...  

1989 ◽  
Vol 264 (22) ◽  
pp. 12752-12753
Author(s):  
J Kuriyan ◽  
L Wong ◽  
M Russel ◽  
P Model

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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