scholarly journals ATP hydrolysis during SOS induction in Escherichia coli.

1986 ◽  
Vol 167 (3) ◽  
pp. 1055-1057 ◽  
Author(s):  
J Barbé ◽  
A Villaverde ◽  
J Cairo ◽  
R Guerrero
Author(s):  
Sebastian Kevekordes ◽  
Volker Mersch-Sundermann ◽  
Christian M Burghaus ◽  
Jan Spielberger ◽  
Heinz H Schmeiser ◽  
...  

2015 ◽  
Vol 290 (34) ◽  
pp. 21032-21041 ◽  
Author(s):  
Naman B. Shah ◽  
Thomas M. Duncan

F-type ATP synthases are rotary nanomotor enzymes involved in cellular energy metabolism in eukaryotes and eubacteria. The ATP synthase from Gram-positive and -negative model bacteria can be autoinhibited by the C-terminal domain of its ϵ subunit (ϵCTD), but the importance of ϵ inhibition in vivo is unclear. Functional rotation is thought to be blocked by insertion of the latter half of the ϵCTD into the central cavity of the catalytic complex (F1). In the inhibited state of the Escherichia coli enzyme, the final segment of ϵCTD is deeply buried but has few specific interactions with other subunits. This region of the ϵCTD is variable or absent in other bacteria that exhibit strong ϵ-inhibition in vitro. Here, genetically deleting the last five residues of the ϵCTD (ϵΔ5) caused a greater defect in respiratory growth than did the complete absence of the ϵCTD. Isolated membranes with ϵΔ5 generated proton-motive force by respiration as effectively as with wild-type ϵ but showed a nearly 3-fold decrease in ATP synthesis rate. In contrast, the ϵΔ5 truncation did not change the intrinsic rate of ATP hydrolysis with membranes. Further, the ϵΔ5 subunit retained high affinity for isolated F1 but reduced the maximal inhibition of F1-ATPase by ϵ from >90% to ∼20%. The results suggest that the ϵCTD has distinct regulatory interactions with F1 when rotary catalysis operates in opposite directions for the hydrolysis or synthesis of ATP.


2021 ◽  
Vol 1 (19) ◽  
pp. 268-269
Author(s):  
A.Yu. Skorokhodova ◽  
V.G. Debabov

The feasibility of the application of enforced ATP hydrolysis to ensure anaerobic functioning of Escherichia coli strain producing butyric acid through the inverted fatty acid beta-oxidation pathway as a full-cell biocatalyst has been demonstrated.


1985 ◽  
Vol 201 (3) ◽  
pp. 525-528 ◽  
Author(s):  
Abdul M. Chaudhury ◽  
Gerald R. Smith

2007 ◽  
Vol 4 (1) ◽  
pp. 53-56 ◽  
Author(s):  
Brittany A Morrison ◽  
Daniel H Shain

Disparate psychrophiles (e.g. glacier ice worms, bacteria, algae and fungi) elevate steady-state intracellular ATP levels as temperatures decline, which has been interpreted as a compensatory mechanism to offset reductions in molecular motion and Gibb's free energy of ATP hydrolysis. In this study, we sought to manipulate steady-state ATP levels in the mesophilic bacterium, Escherichia coli , to investigate the relationship between cold temperature survivability and elevated intracellular ATP. Based on known energetic pathways and feedback loops, we targeted the AMP nucleotidase ( amn ) gene, which is thought to encode the primary AMP degradative enzyme in prokaryotes. By knocking out amn in wild-type E. coli DY330 cells using recombineering methodology, we generated a mutant (AMNk) that elevated intracellular ATP levels by more than 30% across its viable temperature range. As temperature was lowered, the relative ATP disparity between AMNk and DY330 cells increased to approximately 66% at 10°C, and was approximately 100% after storage at 0°C for 5–7 days. AMNk cells stored at 0°C for 7 days displayed approximately fivefold higher cell viability than wild-type DY330 cells treated in the same manner.


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