Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Crude cytoplasmic extracts prepared from HeLa cells actively incorporate amino acids but show little initiation of new peptides (as seen by labeling of N-terminal amino acids). In contrast, extracts prepared from cells subjected to prior inhibition of protein synthesis show a significant amount of polypeptide initiation indicated by formation of peptides with radioactive N-terminal methionine. The same result was obtained whether prior inhibition occurred with cycloheximide or by starvation for an essential amino acid. Cellular response to suppression of protein synthesis appears to be mediated through production of RNA, since it is inhibited by actinomycin but appears in the presence of cycloheximide. The crude extracts continue initiating new polypeptides for at least 10 min in vitro. It is postulated that enhancement of in vitro initiation described here is related to the apparent stimulation of initiation of translation seen in vivo.
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PMID:Stimulation of polypeptide initiation in vitro after protein synthesis inhibition in vivo in HeLa cells. 451 79

The rates of elongation of beta-galactosidase and its messenger ribonucleic acid (RNA) were estimated in a polyamine-deficient mutant of Escherichia coli through an analysis of the kinetics of enzyme induction. The chain growth of beta-galactosidase was calculated from the time required after the appearance of an amino terminal fragment of 60 amino acids (auto-alpha) until completed enzyme began to accumulate. The elongation rate of beta-galactosidase messenger RNA was estimated from the time after induction at which streptolydigen-resistant, enzyme-forming capacity first appeared. Upon polyamine starvation, the rate of polypeptide elongation slowed from 17 to 10 amino acids per s and the messenger RNA elongation rate decreased from 47 to 30 nucleotides per s. These reductions in polymerization rates were proportional to the decrease in cellular growth rate produced by polyamine starvation. It was concluded that, although it is quite unlikely that polyamine levels are involved in regulation of cell growth, they may be acting as cofactors in the synthesis of RNA or protein, or both.
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PMID:Influence of polyamine limitation on the chain growth rates of beta-galactosidase and of its messenger ribonucleic acid. 458 42

The rate of polypeptide chain elongation during steady-state, polyamine-limited growth of a mutant of Escherichia coli was measured by two independent techniques. Analysis of polysome patterns gave values of 17.5 and 9.5 amino acids per s at 37 C in unstarved and polyamine-limited cells, respectively. From the kinetics of entry of labeled amino acids into polypeptides of defined molecular weights, values at 30 C of 10.1 and 5.8 amino acids per s were obtained for unstarved and polyamine-limited cultures, respectively. Correction of these values to 37 C resulted in rates of 15.0 and 8.7 amino acids per s. These results support the previous conclusion, based on the kinetics of beta-galactosidase induction, that polyamine starvation decreases the rate of protein synthesis by limiting the velocity of polypeptide chain elongation.
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PMID:Polyamine limitation of growth slows the rate of polypeptide chain elongation in Escherichia coli. 460 21

A system for screening Escherichia coli temperature-sensitive mutants is described. The system involves glucose starvation and minimizes ambiguities introduced by the interdependencies of macromolecular synthesis during balanced growth. The system permits the quick recognition of protein synthesis mutants and their classification into two general catagories. Complete protein synthesis mutants are unable to make any polypeptide material, whereas partial protein synthesis mutants are able to produce inactive proteins. The phenotypes of several mutants are described.
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PMID:Screening of Escherichia coli temperature-sensitive mutants by pretreatment with glucose starvation. 486 51

Extracellular cyclic-nucleotide phosphodiesterase of Dictyostelium discoideum has previously been purified and characterized [Orlow et al. (1981) J. Biol. Chem. 256, 7620-7627]. Antisera have been raised against the purified enzyme. Following cell-free translation of RNA extracted from cells at various stages of development and immunoprecipitation with anti-phosphodiesterase serum, cAMP phosphodiesterase synthesized in vitro and labeled with L-[35S]methionine can be detected by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and fluorography. The cell-free translation product is an Mr-48 000 polypeptide and can be immunoprecipitated with antiserum raised against active Mr-50 000 cAMP phosphodiesterase or antiserum raised against heat-denatured cAMP phosphodiesterase. Purified native cAMP phosphodiesterase blocks immunoprecipitation of the cAMP-phosphodiesterase polypeptide synthesized in vitro. A detectable level of cAMP-phosphodiesterase mRNA is present in axenically grown cells. After starvation of the cells in phosphate buffer for 1 h an increase of translatable cAMP-phosphodiesterase mRNA occurs, followed by a decrease and another increase. When cells are starved in the presence of the slowly hydrolyzed cAMP analogue, adenosine 3',5'-thiophosphate, the level of translatable cAMP-phosphodiesterase mRNA increases about tenfold and does not show a temporary decline. A maximum of 0.015% of the total acid-insoluble radioactivity is incorporated into the Mr-48 000 cAMP-phosphodiesterase polypeptide.
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PMID:Developmental regulation of the cyclic-nucleotide-phosphodiesterase mRNA of Dictyostelium discoideum. Analysis by cell-free translation and immunoprecipitation. 608 52

We have studied the parameters of protein synthesis in a number of Escherichia coli strains after a shift-down from glucose-minimal to succinate-minimal medium. One group of strains, including K-12(lambda) (ATCC 10798) and NF162, showed a postshift translational yield of 50 to 65% and a 2- to 2.5-fold increase in the functional lifetime of general messenger ribonucleic acid. There was no change in the lag time for beta-galactosidase induction in these strains after the shift-down. A second group, including W1 and W2, showed no reduction in translational yield, no change in the functional lifetime of messenger ribonucleic acid, and a 50% increase in the lag time for beta-galactosidase induction. Evidence is presented which indicates that this increased lag time is not the result of a decreased rate of polypeptide chain propagation. A third group of strains, including NF161, CP78, and NF859, showed an intermediate pattern: translational yield was reduced to about 75% of normal, and the messenger ribonucleic acid functional lifetime was increased by about 50%. Calculation of the relative postshift rates of translational initiation gave about 0.2, 1.0, and 0.5, respectively, for the three groups. There was no apparent correlation between the ability to control translation and the genotypes of these strains at the relA, relX, or spoT loci. Measurements of the induction lag for beta-galactosidase during short-term glucose starvation or after a down-shift induced by alpha-methylglucoside indicated that these regimens elicit responses that are physiologically distinct from those elicited by a glucose-to-succinate shift-down.
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PMID:Control of protein synthesis in Escherichia coli: strain differences in control of translational initiation after energy source shift-down. 615 75

The effects of two polypeptide antibiotics, polymixin B and gramicidin S, on the intracellular pool size and turnover of guanosine tetraphosphate (ppGpp) were analyzed in stringent (relA+) and relaxed (relA) strains of Escherichia coli. When either one of these two drugs was added to stringent bacteria cultures at a final concentration that blocked protein and RNA synthesis, ppGpp was found to accumulate. Under similar conditions of inhibition of macromolecular synthesis, ppGpp also appeared to accumulate in relaxed bacteria. Moreover, in either type of strain, no significant accumulation of guanosine pentaphosphate (pppGpp) could be detected upon drug treatment. It was, therefore, concluded that polymixin and gramicidin elicit ppGpp accumulation through a mechanism independent of the relA gene product and, consequently, quite distinct from the stringent control system triggered by amino acid starvation. Further experiments performed by using tetracycline as an inhibitor of ppGpp synthesis, showed that the increase in the level of this nucleotide induced by drug action was due, in fact, to a strong restriction of its degradation rate.
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PMID:Accumulation of guanosine tetraphosphate induced by polymixin and gramicidin in Escherichia coli. 618 93

When Escherichia coli cells are treated with either polymixin or gramicidin at concentrations that block protein and RNA synthesis, they accumulate a significant amount of guanosine tetraphosphate ppGpp. Such accumulation occurs in stringent (relA+) as well as in relaxed (relA) strains and no guanosine pentaphosphate pppGpp is then detected within the cells. These observations suggest that polypeptide antibiotics elicit ppGpp formation through a mechanism different from the stringent control system triggered by amino acid starvation of bacteria. Experiments based on tetracycline action indicate, moreover, that the accumulation of ppGpp under polymixin or gramicidin treatment is connected with a strong restriction of the degradation rate of this nucleotide.
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PMID:A study of bacterial response to polypeptide antibiotics. 619 Jun 78

The rate of protein synthesis in skeletal muscle is greatly decreased in response to diabetes and starvation. Analysis of polyribosome profiles indicates that polypeptide-chain initiation is impaired under these conditions. To identify the step in initiation that is affected, we assayed the incorporation of [35S]methionyl-tRNAfMet into [35S]methionyl-tRNAfMet . 40S-ribosomal-subunit initiation complexes in cell-free extracts based on postmitochondrial supernatants prepared from gastrocnemius muscle. Extracts from either starved or diabetic rats were 30-40% less active in forming these complexes compared with those derived from fed or insulin-maintained controls respectively. This change could be reversed by treatment of either starved or diabetic rats with insulin in vivo 30 min before death. Formation of 40S initiation complexes by extracts from either fed or starved rats could be stimulated by the addition of exogenous purified initiation factor eIF-2, but extracts from starved or diabetic rats were more sensitive than controls to stimulation by low concentrations of the factor. These results provide evidence for the acute regulation by insulin of protein synthesis in skeletal muscle at the level of polypeptide-chain initiation, and suggest that in this tissue, as in certain other eukaryotic systems, control of initiation appears to be mediated by changes in the activity of initiation factor eIF-2.
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PMID:Effects of starvation, diabetes and acute insulin treatment on the regulation of polypeptide-chain initiation in rat skeletal muscle. 621 77

Incorporation of 5-bromodeoxyuridine (5-BUdR) into nuclear DNA severely interrupts the life cycle of Dictyostelium discoideum after the first generation of growth. Loose cellular aggregates are then formed, but no spore or stalk cells are detectable and no other morphological transformations are observed. The perturbation of gene expression in the life cycle has been studied at the protein level by two-dimensional gel electrophoresis after pulse labelling with 35S-methionine and also by changes in the patterns of polysomal messenger RNA population. The latter was monitored by hybridisation studies using specific cDNA probes for "vegetative" and "18 hr" messenger RNAs. In the presence of 5-BUdR major anomalies in polypeptide synthesis were observed after the loose aggregation stage. Some vegetative polypeptides, including actin, which are normally abundant only during growth to the aggregation stage, are oversynthesised during the period 12-24 hr after starvation. In this same interval the normal decline in the abundance of vegetative mRNA species was not observed. In marked contrast virtually half the normal "18 hr-specific polypeptides" were poorly synthesised. Likewise, the normal increase in abundance of the corresponding "18 hr-specific" poly A + RNA species in the polysomes did not occur. No major alteration in the timing of the appearance of new macromolecules during the cell cycle was observed in spite of extensive modification of gene expression by the incorporation of 5-BUdR into genomic DNA.
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PMID:Changes in protein synthesis and in RNA poly A+ population after treatment of Dictyostelium amoebae by 5-bromo-2'-deoxyuridine. 624 33


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