scholarly journals The ms2io6A37 Modification of tRNA inSalmonella typhimurium Regulates Growth on Citric Acid Cycle Intermediates

1998 ◽  
Vol 180 (12) ◽  
pp. 3144-3151 ◽  
Author(s):  
Britt C. Persson ◽  
Ólafur Ólafsson ◽  
Hans K. Lundgren ◽  
Lars Hederstedt ◽  
Glenn R. Björk
Keyword(s):  
Escherichia Coli ◽  
Citric Acid ◽  
Salmonella Typhimurium ◽  
Gene Product ◽  
Respiratory Chain ◽  
Citric Acid Cycle ◽  
Dicarboxylic Acids ◽  
Acid Cycle ◽  
E Coli ◽  
Isopentenyl Adenosine

ABSTRACT The modified nucleoside 2-methylthio-N-6-isopentenyl adenosine (ms2i6A) is present in position 37 (adjacent to and 3′ of the anticodon) of tRNAs that read codons beginning with U except tRNA I,V Ser inEscherichia coli. In Salmonella typhimurium, 2-methylthio-N-6-(cis-hydroxy)isopentenyl adenosine (ms2io6A; also referred to as 2-methylthio cis-ribozeatin) is found in tRNA, most likely in the species that have ms2i6A in E. coli. Mutants (miaE) of S. typhimurium in which ms2i6A hydroxylation is blocked are unable to grow aerobically on the dicarboxylic acids of the citric acid cycle. Such mutants have normal uptake of dicarboxylic acids and functional enzymes of the citric acid cycle and the aerobic respiratory chain. The ability of S. typhimurium to grow on succinate, fumarate, and malate is dependent on the state of modification in position 37 of those tRNAs normally having ms2io6A37 and is not due to a second cellular function of tRNA (ms2io6A37)hydroxylase, themiaE gene product. We suggest that S. typhimurium senses the hydroxylation status of the isopentenyl group of the tRNA and will grow on succinate, fumarate, or malate only if the isopentenyl group is hydroxylated.

scholarly journals Functions of the Membrane-Associated and Cytoplasmic Malate Dehydrogenases in the Citric Acid Cycle ofEscherichia coli

2000 ◽  
Vol 182 (24) ◽  
pp. 6892-6899 ◽  
Author(s):  
Michel E. van der Rest ◽  
Christian Frank ◽  
Douwe Molenaar
Keyword(s):  
Citric Acid ◽  
Malic Enzyme ◽  
Citric Acid Cycle ◽  
Wild Type ◽  
Batch Cultures ◽  
Acid Cycle ◽  
E Coli ◽  
Link Type ◽  
Phosphoenolpyruvate Synthase ◽  
Rates Of Growth

ABSTRACT Oxidation of malate to oxaloacetate in Escherichia colican be catalyzed by two enzymes: the well-known NAD-dependent malate dehydrogenase (MDH; EC 1.1.1.37 ) and the membrane-associated malate:quinone-oxidoreductase (MQO; EC 1.1.99.16 ), encoded by the genemqo (previously called yojH). Expression of themqo gene and, consequently, MQO activity are regulated by carbon and energy source for growth. In batch cultures, MQO activity was highest during exponential growth and decreased sharply after onset of the stationary phase. Experiments with the β-galactosidase reporter fused to the promoter of the mqo gene indicate that its transcription is regulated by the ArcA-ArcB two-component system. In contrast to earlier reports, MDH did not repressmqo expression. On the contrary, MQO and MDH are active at the same time in E. coli. For Corynebacterium glutamicum, it was found that MQO is the principal enzyme catalyzing the oxidation of malate to oxaloacetate. These observations justified a reinvestigation of the roles of MDH and MQO in the citric acid cycle of E. coli. In this organism, a defined deletion of the mdh gene led to severely decreased rates of growth on several substrates. Deletion of the mqo gene did not produce a distinguishable effect on the growth rate, nor did it affect the fitness of the organism in competition with the wild type. To investigate whether in an mqo mutant the conversion of malate to oxaloacetate could have been taken over by a bypass route via malic enzyme, phosphoenolpyruvate synthase, and phosphenolpyruvate carboxylase, deletion mutants of the malic enzyme genessfcA and b2463 (coding for EC 1.1.1.38 and EC1.1.1.40 , respectively) and of the phosphoenolpyruvate synthase (EC2.7.9.2 ) gene pps were created. They were introduced separately or together with the deletion of mqo. These studies did not reveal a significant role for MQO in malate oxidation in wild-type E. coli. However, comparing growth of themdh single mutant to that of the double mutant containingmdh and mqo deletions did indicate that MQO partly takes over the function of MDH in an mdh mutant.

The Glyoxylate Shunt, 60 Years On

2018 ◽  
Vol 72 (1) ◽  
pp. 309-330 ◽  
Author(s):  
Stephen K. Dolan ◽  
Martin Welch
Keyword(s):  
Citric Acid ◽  
Citric Acid Cycle ◽  
Tca Cycle ◽  
Oxidative Decarboxylation ◽  
Glyoxylate Shunt ◽  
Cellular Functions ◽  
Acid Cycle ◽  
E Coli ◽  
80Th Anniversary ◽  
The Tca Cycle

2017 marks the 60th anniversary of Krebs’ seminal paper on the glyoxylate shunt (and coincidentally, also the 80th anniversary of his discovery of the citric acid cycle). Sixty years on, we have witnessed substantial developments in our understanding of how flux is partitioned between the glyoxylate shunt and the oxidative decarboxylation steps of the citric acid cycle. The last decade has shown us that the beautifully elegant textbook mechanism that regulates carbon flux through the shunt in E. coli is an oversimplification of the situation in many other bacteria. The aim of this review is to assess how this new knowledge is impacting our understanding of flux control at the TCA cycle/glyoxylate shunt branch point in a wider range of genera, and to summarize recent findings implicating a role for the glyoxylate shunt in cellular functions other than metabolism.

Inactivation of Listeria monocytogenes, Escherichia coli O157:H7, and Salmonella Typhimurium with Compounds Available in Households

2009 ◽  
Vol 72 (6) ◽  
pp. 1201-1208 ◽  
Author(s):  
HUA YANG ◽  
PATRICIA A. KENDALL ◽  
LYDIA MEDEIROS ◽  
JOHN N. SOFOS
Keyword(s):  
Escherichia Coli ◽  
Hydrogen Peroxide ◽  
Acetic Acid ◽  
Listeria Monocytogenes ◽  
Citric Acid ◽  
Salmonella Typhimurium ◽  
Initial Temperature ◽  
Escherichia Coli O157 ◽  
E Coli ◽  
Log Reduction

Solutions of selected household products were tested for their effectiveness against Listeria monocytogenes, Escherichia coli O157:H7, and Salmonella Typhimurium. Hydrogen peroxide (1.5 and 3%), vinegar (2.5 and 5% acetic acid), baking soda (11, 33, and 50% sodium bicarbonate), household bleach (0.0314, 0.0933, and 0.670% sodium hypochlorite), 5% acetic acid (prepared from glacial acetic acid), and 5% citric acid solutions were tested against the three pathogens individually (five-strain composites of each, 108 CFU/ml) by using a modified AOAC International suspension test at initial temperatures of 25 and 55°C for 1 and 10 min. All bleach solutions (pH 8.36 to 10.14) produced a >5-log reduction of all pathogens tested after 1 min at 25°C, whereas all baking soda solutions (pH 7.32 to 7.55) were ineffective (<1-log reduction) even after 10 min at an initial temperature of 55°C. After 1 min at 25°C, 3% hydrogen peroxide (pH 2.75) achieved a >5-log reduction of both Salmonella Typhimurium and E. coli O157:H7, whereas undiluted vinegar (pH 2.58) had a similar effect only against Salmonella Typhimurium. Compared with 1 min at 25°C, greater reductions of L. monocytogenes (P < 0.05) were obtained with all organic acid and hydrogen peroxide treatments after 10 min at an initial temperature of 55°C. The efficacies of household compounds against all tested pathogens decreased in the following order: 0.0314% sodium hypochlorite > 3% hydrogen peroxide > undiluted vinegar and 5% acetic acid > 5% citric acid > baking soda (50% sodium bicarbonate). The sensitivity of the tested pathogens to all tested household compounds followed the sequence of Salmonella Typhimurium > E. coli O157: H7 > L. monocytogenes.

scholarly journals ATP oscillation caused by Gradual Entry of Substrates within Mitochondria

2021 ◽  
Author(s):  
Taketoshi Hideshima ◽  
Mikie Nishimura
Keyword(s):  
Citric Acid ◽  
Respiratory Chain ◽  
Citric Acid Cycle ◽  
Permeation Rate ◽  
Oscillatory Reaction ◽  
Dialysis Membrane ◽  
Acid Cycle ◽  
Oscillatory Reactions ◽  
Suitable Combination ◽  
Living Organisms

Abstract The gradual entry of the substrate into enzyme solution causes the oscillatory reaction. We proved this by using dialysis membrane as a means of gradual entry of substrates 7. It was considered that a suitable combination of permeation rate through membrane of the substrate and rate constants for catalytic reaction regulates the oscillation. It was suggested that such oscillatory reactions also should occur in actual living organisms. On the basis of this suggestion, we explored the oscillatory reaction within mitochondria, because many reactions in mitochondria also occur in the mediation of membrane. We found that the gradual entry of pyruvate together with ADP caused the oscillations of both NADH and ATP within mitochondria. Likewise, the gradual entry of NAD+ and malate together with ADP caused the oscillations of NADH and of ATP. At the same time, pH oscillation within mitochondria was also observed. Besides the experiment with mitochondria, we also investigated oscillations of NADH and the other intermediates using dialysis membrane both in the citric acid cycle and in the respiratory chain. Putting these together, we concluded that the oscillatory reactions caused by the gradual entry of pyruvate occur continuously both in the citric acid cycle and in the respiratory chain and is taken over finally by the reaction of ATP synthase in the oxidative phosphorylation, inducing the oscillation of ATP. Furthermore, it was found that oscillations occurred without going through the citric acid cycle when NAD+ and malate were used instead of pyruvate.

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