Bile Acid Synthesis, Metabolism and Biological Functions
Protein synthesis rate was determined from incorporation of l-[2,6 3 H]-phenylalanine ..
Bile Acid Synthesis and Utilization
Escherichia coli Q13 was infected with bacteriophage Q beta and subjected to energy source shift-down (from glucose-minimal to succinate-minimal medium) 20 min after infection. Production of progeny phage was about fourfold slower in down-shifted cultures than in the cultures in glucose medium. Shift-down did not affect the rate of phage RNA replication, as measured by the rate of incorporation of [14C]uracil in the presence of rifampin, with appropriate correction for the reduced entry of exogenous uracil into the UTP pool. Phage coat protein synthesis was three- to sixfold slower in down-shifted cells than in exponentially growing cells, as determined by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The polypeptide chain propagation rate in infected cells was unaffected by the down-shift. Thus, the reduced production of progeny phage in down-shifted cells appears to result from control of phage protein synthesis at the level of initiation of translation. The reduction in the rate of Q beta coat protein synthesis is comparable to the previously described reduction in the rate of synthesis of total E. coli protein and of beta-galactosidase, implying that the mechanism which inhibits translation in down-shifted cells is neither messenger specific nor specific for 5' proximal cistrons. The intracellular ATP pool size was nearly constant after shift-down; general energy depletion is thus not a predominant factor. The GTP pool, by contrast, declined by about 40%. Also, ppGpp did not accumulate in down-shifted, infected cells in the presence of rifampin, indicating that ppGpp is not the primary effector of this translational inhibition.
...prised 24–54% of the top 50 most highly expressed genes in each clinical isolate. It is well established that E. coli rRNA and ribosomal protein mRNA synthesis increases proportionally to growth rate =-=[38,39]-=-. Consistent with this, the most highly expressed non-ribosomal genes also suggest rapid bacterial growth in vivo (Table 1). Genes encoding transcription and translation machinery (infC, yfiA, rpoA, r...
The end products of cholesterol utilization are the bile acids
... discrepancy between them is significant. The rate of spc mRNA synthesis relative to the rate of total mRNA synthesis (rspc/rm) has been reported to increase with increasing growth rate similar to ar =-=(13, 21)-=-. This has suggested that r-protein synthesis is primarily regulated at the transcriptional level, so that the translational regulation only provides a “fine-tuning” to accurately adjust r-protein syn...
Cultured tobacco cells (Nicotiana tabacum L. cv. Wisconsin 38) synthesize a predominant 26-kDa protein upon exposure to abscisic acid (ABA). ABA also accelerates the rate of adaptation of unadapted cells to NaCl stress. The ABA-induced 26-kDa protein is immunologically cross-reactive to, and produces a similar pattern of peptides after partial proteolysis as, the major 26-kDa protein associated with NaCl adaptation. Both have pI values of >8.2. The synthesis of the ABA-induced 26-kDa protein is transient unless the cells are simultaneously exposed to NaCl stress. There is an association between increased intracellular accumulation of ABA during cell growth and commencement of synthesis of the 26-kDa protein. ABA induces the synthesis of an immunologically cross-reactive 26-kDa protein in cultured cells of several plant species. In tobacco plants, synthesis of the 26-kDa protein could be detected in several tissues but the highest level of expression was seen in outer stem tissue. In root tissues, exogenous ABA greatly stimulated the synthesis of 26-kDa protein as compared to outer stem tissue and leaf. We suggest that ABA is involved in the normal induction of the synthesis of 26-kDa protein and that the presence of NaCl is necessary for the protein to accumulate.
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