scholarly journals Genetic evidence that genes fdhD and fdhE do not control synthesis of formate dehydrogenase-N in Escherichia coli K-12.

1991 ◽  
Vol 173 (14) ◽  
pp. 4417-4423 ◽  
Author(s):  
V Stewart ◽  
J T Lin ◽  
B L Berg
Keyword(s):  
Escherichia Coli ◽  
Formate Dehydrogenase ◽  
Genetic Evidence ◽  
Control Synthesis ◽  
K 12

scholarly journals Structural genes for nitrate-inducible formate dehydrogenase in Escherichia coli K-12.

Genetics ◽  
1990 ◽  
Vol 125 (4) ◽  
pp. 691-702 ◽  
Author(s):  
B L Berg ◽  
V Stewart
Keyword(s):  
Escherichia Coli ◽  
Nitrate Reductase ◽  
Formate Dehydrogenase ◽  
Recombinant Dna ◽  
Structural Genes ◽  
Respiratory Pathway ◽  
E Coli ◽  
Formate Oxidation ◽  
Operon Expression ◽  
K 12

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.

scholarly journals Genetic Evidence for an Interaction of the UbiG O-Methyltransferase with UbiX in Escherichia coli Coenzyme Q Biosynthesis

2006 ◽  
Vol 188 (17) ◽  
pp. 6435-6439 ◽  
Author(s):  
Melissa Gulmezian ◽  
Haitao Zhang ◽  
George T. Javor ◽  
Catherine F. Clarke
Keyword(s):  
Escherichia Coli ◽  
Mutant Strain ◽  
Coenzyme Q ◽  
Genetic Evidence ◽  
Deficient Mutant ◽  
Gene Encoding ◽  
K 12

ABSTRACT IS16 is a thiol-sensitive, Q-deficient mutant strain of Escherichia coli. Here, we show that IS16 harbors a mutation in the ubiG gene encoding a methyltransferase required for two O-methylation steps of Q biosynthesis. Complementation of IS16 with either ubiG or ubiX K-12 reverses this phenotype, suggesting that UbiX may interact with UbiG.

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