scholarly journals The torYZ (yecK bisZ) Operon Encodes a Third Respiratory Trimethylamine N-Oxide Reductase inEscherichia coli

2000 ◽  
Vol 182 (20) ◽  
pp. 5779-5786 ◽  
Author(s):  
Stéphanie Gon ◽  
Jean-Claude Patte ◽  
Vincent Méjean ◽  
Chantal Iobbi-Nivol
Keyword(s):  
Escherichia Coli ◽  
Dimethyl Sulfoxide ◽  
Gene Product ◽  
Respiratory System ◽  
Common Ancestor ◽  
Catalytic Properties ◽  
Inescherichia Coli ◽  
Low Levels ◽  
A Minor ◽  
Tmao Reductase

ABSTRACT The bisZ gene of Escherichia coli was previously described as encoding a minor biotin sulfoxide (BSO) reductase in addition to the main cytoplasmic BSO reductase, BisC. In this study, bisZ has been renamed torZ based on the findings that (i) the torZ gene product, TorZ, is able to reduce trimethylamine N-oxide (TMAO) more efficiently than BSO; (ii) although TorZ is more homologous to BisC than to the TMAO reductase TorA (63 and 42% identity, respectively), it is located mainly in the periplasm as is TorA; (iii)torZ belongs to the torYZ operon, and the first gene, torY (formerly yecK), encodes a pentahemic c-type cytochrome homologous to the TorC cytochrome of the TorCAD respiratory system. Furthermore, the torYZ operon encodes a third TMAO respiratory system, with catalytic properties that are clearly different from those of the TorCAD and the DmsABC systems. ThetorYZ and the torCAD operons may have diverged from a common ancestor, but, surprisingly, notorD homologue is found in the sequences aroundtorYZ. Moreover, the torYZ operon is expressed at very low levels under the conditions tested, and, in contrast to torCAD, it is not induced by TMAO or dimethyl sulfoxide.

A modified uridine in the first position of the anticodon of a minor species of arginine tRNA, the argU gene product, from Escherichia coli

1993 ◽  
Vol 216 (2) ◽  
pp. 369-375 ◽  
Author(s):  
Kensaku SAKAMOTO ◽  
Gota KAWAI ◽  
Tatsuya NIIMI ◽  
Takahiko SATOH ◽  
Mitsuo SEKINE ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Gene Product ◽  
A Minor

scholarly journals Enzymatic and physiological properties of the tungsten-substituted molybdenum TMAO reductase from Escherichia coli

1999 ◽  
Vol 32 (1) ◽  
pp. 159-168 ◽  
Author(s):  
Jean Buc ◽  
Claire-Lise Santini ◽  
Roger Giordani ◽  
Mirjam Czjzek ◽  
Long-Fei Wu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Physiological Properties ◽  
Tmao Reductase

scholarly journals Long-Term Experimental Evolution in Escherichia coli. IV. Targets of Selection and the Specificity of Adaptation

Genetics ◽  
1996 ◽  
Vol 143 (1) ◽  
pp. 15-26 ◽  
Author(s):  
Michael Travisano ◽  
Richard E Lenski
Keyword(s):  
Escherichia Coli ◽  
Experimental Evolution ◽  
Common Ancestor ◽  
The Novel ◽  
Physiological Mechanisms ◽  
Outer Membranes ◽  
Limiting Nutrient ◽  
Novel Environments ◽  
Uptake Mechanisms

Abstract This study investigates the physiological manifestation of adaptive evolutionary change in 12 replicate populations of Escherichia coli that were propagated for 2000 generations in a glucose-limited environment. Representative genotypes from each population were assayed for fitness relative to their common ancestor in the experimental glucose environment and in 11 novel single-nutrient environments. After 2000 generations, the 12 derived genotypes had diverged into at least six distinct phenotypic classes. The nutrients were classified into four groups based upon their uptake physiology. All 12 derived genotypes improved in fitness by similar amounts in the glucose environment, and this pattern of parallel fitness gains was also seen in those novel environments where the limiting nutrient shared uptake mechanisms with glucose. Fitness showed little or no consistent improvement, but much greater genetic variation, in novel environments where the limiting nutrient differed from glucose in its uptake mechanisms. This pattern of fitness variation in the novel nutrient environments suggests that the independently derived genotypes adapted to the glucose environment by similar, but not identical, changes in the physiological mechanisms for moving glucose across both the inner and outer membranes.

A multi-institutional outbreak of New Delhi metallo-β-lactamase–producing Escherichia coli with subsequent acquisition of the Klebsiella pneumoniae carbapenemase gene

2020 ◽  
pp. 1-4
Author(s):  
Ester Solter ◽  
Jason C. Kwong ◽  
Aaron Walton ◽  
Norelle Sherry ◽  
Benjamin P. Howden ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Klebsiella Pneumoniae ◽  
Common Ancestor ◽  
Sequence Type ◽  
Second Phase ◽  
New Delhi ◽  
Genetic Sequencing ◽  
Klebsiella Pneumoniae Carbapenemase ◽  
Carbapenemase Gene

Abstract We characterized 57 isolates from a 2-phase clonal outbreak of New Delhi metallo-β-lactamase–producing Eschericha coli, involving 9 Israeli hospitals; all but 1 isolate belonged to sequence-type (ST) 410. Most isolates in the second phase harbored blaKPC-2 in addition to blaNDM-5. Genetic sequencing revealed most dual-carbapenemase–producing isolates to be monophyletically derived from a common ancestor.

scholarly journals Structural and catalytic properties of a deletion derivative (delta 133-157) of Escherichia coli adenylate kinase

1991 ◽  
Vol 266 (17) ◽  
pp. 10781-10786
Author(s):  
T. Rose ◽  
M. Brune ◽  
A. Wittinghofer ◽  
K. Le Blay ◽  
W.K. Surewicz ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Adenylate Kinase ◽  
Catalytic Properties ◽  
Deletion Derivative

scholarly journals In vitro heme O synthesis by the cyoE gene product from Escherichia coli.

1993 ◽  
Vol 268 (35) ◽  
pp. 26041-26044
Author(s):  
K Saiki ◽  
T Mogi ◽  
K Ogura ◽  
Y Anraku
Keyword(s):  
Escherichia Coli ◽  
Gene Product
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