scholarly journals Role of the phosphotransferase system inEscherichia colistrains deficient in hexose phosphate transport

1994 ◽  
Vol 116 (2) ◽  
pp. 209-214 ◽  
Author(s):  
Valérie Dumay ◽  
Martine Crasnier
1984 ◽  
Vol 247 (4) ◽  
pp. F582-F587 ◽  
Author(s):  
S. R. Gullans ◽  
P. C. Brazy ◽  
L. J. Mandel ◽  
V. W. Dennis

Studies of phosphate transport in the proximal tubule have recently focused on interactions with cellular metabolism. The present studies demonstrate that two fatty acids, valerate and butyrate, and two tricarboxylic acid cycle intermediates, succinate and malate, stimulate net phosphate transport in the rabbit proximal tubule by 34-117%. Valerate had no effect on the total uptake of inorganic [32P]phosphate into suspensions of proximal tubules but did enhance the initial rate of influx. Net fluid transport was unaffected by these substrates although glucose absorption increased by 10-15% following the addition of either valerate or succinate. Since valerate, butyrate, and succinate are known to stimulate gluconeogenesis and respiration, we evaluated the role of gluconeogenesis in the stimulation of phosphate transport. The addition of 3-mercaptopicolinate (1 mM), an inhibitor of gluconeogenesis, did not alter phosphate transport, nor did it prevent the valerate-induced stimulation of phosphate transport. We conclude that valerate, butyrate, succinate, and malate enhance phosphate transport by the proximal convoluted tubule. This action appears to be unrelated to effects on gluconeogenesis and may be related to close links between phosphate transport and oxidative metabolism.


2019 ◽  
Vol 29 (1-6) ◽  
pp. 10-26 ◽  
Author(s):  
Thanh Nguyen Cao ◽  
Philippe Joyet ◽  
Francine Moussan Désirée Aké ◽  
Eliane Milohanic ◽  
Josef Deutscher

<b><i>Background:</i></b> Many bacteria transport cellobiose via a phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In <i>Listeria monocytogenes</i>, two pairs of soluble PTS components (EIIA<sup>Cel1</sup>/EIIB<sup>Cel1</sup> and EIIA<sup>Cel2</sup>/EIIB<sup>Cel2</sup>) and the permease EIIC<sup>Cel1</sup> were suggested to contribute to cellobiose uptake. Interestingly, utilization of several carbohydrates, including cellobiose, strongly represses virulence gene expression by inhibiting PrfA, the virulence gene activator. <b><i>Results:</i></b> The LevR-like transcription regulator CelR activates expression of the cellobiose-induced PTS operons <i>celB1</i>-<i>celC1</i>-<i>celA1</i>, <i>celB2</i>-<i>celA2</i>, and the EIIC-encoding monocistronic <i>celC2</i>. Phosphorylation by P∼His-HPr at His550 activates CelR, whereas phosphorylation by P∼EIIB<sup>Cel1</sup> or P∼EIIB<sup>Cel2</sup> at His823 inhibits it. Replacement of His823 with Ala or deletion of both <i>celA</i> or <i>celB</i> genes caused constitutive CelR regulon expression. Mutants lacking EIIC<sup>Cel1</sup>, CelR or both EIIA<sup>Cel</sup> exhibited<i></i>slow cellobiose consumption. Deletion of <i>celC1</i> or <i>celR</i> prevented virulence gene repression by the disaccharide, but not by glucose and fructose. Surprisingly, deletion of both <i>celA</i> genes caused virulence gene repression even during growth on non-repressing carbohydrates. No cellobiose-related phenotype was found for the <i>celC2</i> mutant. <b><i>Conclusion:</i></b> The two EIIA/B<sup>Cel</sup> pairs are similarly efficient as phosphoryl donors in EIIC<sup>Cel1</sup>-catalyzed cellobiose transport and CelR regulation. The permanent virulence gene repression in the <i>celA</i> double mutant further supports a role of PTS<sup>Cel</sup> components in PrfA regulation.


1967 ◽  
Vol 58 (5) ◽  
pp. 1963-1970 ◽  
Author(s):  
R. D. Simoni ◽  
M. Levinthal ◽  
F. D. Kundig ◽  
W. Kundig ◽  
B. Anderson ◽  
...  

1972 ◽  
Vol 17 (4) ◽  
pp. 251-260 ◽  
Author(s):  
A. Knotková ◽  
A. Kotyk

1978 ◽  
Vol 24 (3) ◽  
pp. 203-208
Author(s):  
George W. Dietz Jr.

Glucosamine 6-phosphate was found to be a substrate but not an inducer for the hexose phosphate transport system of Escherichia coli. Wild-type cells grow very poorly on glucosamine 6-phosphate. A mutant was selected that will grow rapidly on glucosamine 6-phosphate because it contains a constitutive hexose phosphate transport system.


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