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Energy Metabolism of Rickettsia typhi : Pools of Adenine Nucleotides and Energy Charge in the Presence and Absence of Glutamate
Author(s) -
Jim C. Williams,
Emilio Weiss
Publication year - 1978
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.134.3.884-892.1978
Subject(s) - energy charge , adenylate kinase , biology , adenine nucleotide , biochemistry , glutamine , nucleotide , intracellular , incubation , glutamate receptor , adenosine triphosphate , adenosine monophosphate , metabolism , amp deaminase , extracellular , adenosine , microbiology and biotechnology , enzyme , amino acid , adenosine deaminase , receptor , gene
The obligate intracellular bacteriumRickettsia typhi was examined for its ability to generate and maintain an adenylate energy charge in an extracellular environment. Freshly purified organisms were incubated, at 34°C and pH 7.4, with or without glutamate and various other metabolites, and the levels of ATP, ADP, and AMP were determined. Of the metabolites tested, glutamate and glutamine were the most effective for the generation of ATP. In the presence of glutamate, there was a rapid increase in the level of ATP, followed by a moderate decrease during 150 min of incubation. The energy charge increased from a level of 0.2 to 0.5 to about 0.7 to 0.75, and then slowly declined to about 0.45 to 0.6. In the absence of glutamate, after an occasional initial surge in ATP level as the temperature was changed from 4 to 34°C, there was a sharp decline in both ATP and energy charge (to 0.1 and sometimes to 0.01). The rickettsiae maintained their ability to regenerate their energy charge upon the addition of glutamate for about 30 min, but this ability declined with further incubation. In contrast toEscherichia coli , the decline in ATP inR. typhi was accompanied by a sharp increase in the level of AMP and the total adenylate pool. No adenine or adenosine was recovered from rickettsiae incubated with labeled AMP, ADP, or ATP. From these experiments and the demonstration reported elsewhere that rickettsiae transport the adenine nucleotides, it can be concluded that the adenylate energy charge inR. typhi is governed by the salvage of the adenine nucleotides rather than their unphosphorylated precursors. Thus,R. typhi undergoes greater shifts in energy charge than other bacteria, a phenomenon which may account for their instability in an extracellular environment. Under optimal conditions the adenylate energy charge ofR. typhi approaches levels that border on those generally regarded as adequate for growth.

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