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- W103060844 abstract "The interdependence of changes in the concentration of adenosine polyphosphates and changes in the pattern of protein synthesis has been investigated in an in vivo unbalanced system, Tetrahymena pyriformis cells that were shifted from growth to starvation conditions. The following events were observed during the first 1–2 hours of starvation: 1. an abrupt inhibition of initiation of protein synthesis (disaggregation of polyribosomes); 2. a preferential synthesis of 7 proteins starting 15–30 min after the shift-down; 3. an unchanged pattern of proteins synthesized by in vitro translation of limiting amounts of poly(A) containing RNA isolated during the first hour of starvation; 4. a transition of ribosomal protein S6 from the non-phosphorylated to a highly phosphorylated state which is not impaired by DNP treatment and complete after about 1 h of starvation; 5. an increase in ATP content from 14 to 21 nmol·mg protein -1 during the first 30 min of starvation, followed by a decrease; 6. a steady increase in Ap 4 A content from an unmeasurable level immediately after the shift to about 40 pmol·mg protein -1 at 1 h of starvation; 7. an immediate increase in Ap 4 A content to about 40 pmol·mg protein -1 in DNP treated cells. The effects of ATP can pragmatically be considered to be turnover effects (hydrolysis of ATP) or concentration effects (binding of ATP and allosteric effects). In the present case, ATP is believed to accumulate passively as the result of a decreased utilization and then actively act as a regulator by virtue of the high concentration. The phosphorylation of the ribosomal protein S6 is considered to part of a mechanism that ensures preferential translation of de novo synthesized mRNA." @default.
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- W103060844 date "1979-01-01" @default.
- W103060844 modified "2023-09-26" @default.
- W103060844 title "RELATION OF PROTEIN SYNTHESIS TO THE CONTENT OF ADENOSINE POLYPHOSPHATES" @default.
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- W103060844 doi "https://doi.org/10.1016/b978-0-12-417580-8.50027-7" @default.
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