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Query: UMLS:C0038187 (starvation)
 24,951 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lipid bilayer experiments were performed with one OmpF-PhoE and several OmpC-PhoE hybrid porins of Escherichia coli K-12. All hybrid pores had approximately the same pore-forming activity, which indicated that the structure of the pores remained essentially unchanged by the genetic manipulation. This result was supported by single-channel experiments because all pores had similar single-channel conductances in potassium chloride. Measurements with other salts indicated a drastic change in the ionic selectivity when the fusion site in the ompC-phoE hybrid genes passed along the sequence of the porins from the N-terminal to the C-terminal end. Selectivity measurements using zero-current membrane potentials showed that the selectivity suddenly changed from anion to cation selectivity when a relatively short portion from the N-terminal end of PhoE was replaced by the corresponding part of OmpC. The replacement of increasing portions led to an increase in the cation selectivity until that of OmpC was reached. The change in the anion to cation selectivity is correlated with exchange of lysine-18 and serine-28 by aspartic acids. The anion selectivity of the phosphate starvation-inducible PhoE porin is closely related to the presence of several lysines spread along the primary sequence of the polypeptide chain.
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PMID:Molecular basis of porin selectivity: membrane experiments with OmpC-PhoE and OmpF-PhoE hybrid proteins of Escherichia coli K-12. 247 Apr 9

Site-directed mutagenesis was performed with the phosphate starvation-inducible outer membrane porin PhoE of Escherichia coli K-12 to study the molecular basis of its anion selectivity. Lysines 18, 29, 64, and 125 were replaced by glutamic acids, and the properties of the mutant porins were investigated in in vivo and in vitro experiments. Lipid bilayer experiments showed that all these mutations had no influence on the pore structure because PhoE and the mutants had the same single channel conductance in KCl solution. Selectivity measurements revealed that the mutations changed the ionic selectivity of PhoE, but the change was dependent on the location of the lysine. Replacement of Lys18 and Lys29 by glutamic acid had a relatively small influence. The effect of the Lys64 substitution was somewhat larger, and the effect of the replacement of Lys125 resulted in the most drastic change in selectivity and in the loss of the interaction of PhoE with polyphosphate, whereas the replacement of the other lysines had no effect on the polyphosphate interaction behavior. The results are consistent with the assumption that the charge spot in PhoE consists of only 1 lysine per monomer, located in position 125 of the primary sequence and probably close to the pore interior.
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PMID:One single lysine residue is responsible for the special interaction between polyphosphate and the outer membrane porin PhoE of Escherichia coli. 247 43

In submerged grown hyphae of Penicillium cyclopium the activities of seven transport systems could be distinguished which share in the uptake of L-arginine, L-glutamic acid, L-phenylalanine and L-leucine. They include the specific systems a (accepting L-arginine and L-lysine), b (L-phenylalanine, L-tyrosine), c (L-glutamic acid) and d (L-leucine), system I (a 'general amino-acid permease') and the low-affinity systems II and III, which accept acidic or basic amino acids, respectively, but also L-phenylalanine. In nutrient-sufficient cells, systems I, II and III remain repressed; uptake is dominated by the specific systems b, c, d and a, the latter reaching its maximum activity. Nitrogen starvation is the most powerful signal for the development of systems I, II and III, whereas, in carbon-starved cells, systems b, c and d reach maximum activities. The development of the general amino-acid permease in nitrogen-starved cells requires both translational and--with a few hours delay--transcriptional events as indicated by the influence of cycloheximide and 5-fluorouracil. The uptake of all amino acids is accompanied by a transient acidification of the cellular interior. Short-time preaccumulation of several anions, such as citrate, alpha-oxo-glutarate, glutamate (but not glutamine), increases the initial rate of amino-acid uptake at a pH above the optimum. Uncouplers inhibit the uptake not only under aerobic but also under anaerobic conditions, where the ATP content is not influenced by these compounds. These findings point to an H+/amino acid symport, which is tightly connected with the recycling of the incoming protons by the plasmalemma H+-ATPase.
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PMID:Kinetic properties, nutrient-dependent regulation and energy coupling of amino-acid transport systems in Penicillium cyclopium. 256 28

The GCN2 protein of Saccharomyces cerevisiae stimulates the expression of amino acid biosynthetic genes under conditions of amino acid starvation by derepressing GCN4, a transcriptional activator of these genes. GCN2 contains sequences homologous to the catalytic domain of protein kinases. We show here that substitution of a highly conserved lysine in the presumed ATP-binding site of this domain impairs the derepression of histidine biosynthetic genes under GCN4 control. This result supports the idea that protein kinase activity is required for GCN2 positive regulatory function. Determination of the nucleotide sequence of the entire GCN2 complementation unit, and measurement of the molecular weight of GCN2 protein expressed in vivo, indicate that GCN2 is a Mr approximately 180,000 protein and contains a Mr approximately 60,000 segment homologous to histidyl-tRNA synthetases (HisRSs) juxtaposed to the protein kinase domain. Several two-codon insertion mutations in the HisRS-related coding sequences inactivate GCN2 regulatory function. Based on these results, we propose that the GCN2 HisRS domain responds to the presence of uncharged tRNA by activating the adjacent protein kinase moiety, thus providing a means of coupling GCN2-mediated derepression of GCN4 expression to the availability of amino acids.
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PMID:Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability. 266 Jan 41

In this article we summarize evidence for a pathway by which cytosolic proteins can be selectively taken up and degraded within lysosomes. Serum deprivation of cells in culture activates this pathway, and only proteins that contain peptide sequences related to KFERQ (lysine, phenylalanine, glutamic acid, arginine, glutamine) are degraded at enhanced rates. Approximately 30% of intracellular proteins contain such peptide sequences, and we speculate about the physiological relevance of the selective degradation of these proteins in response to serum withdrawal. Several rat tissues also contain proteins with peptide sequences related to KFERQ, and the amount of these proteins is reduced in response to starvation. Finally, we present recent results suggesting that this selective uptake of cytosolic proteins by lysosomes is not through classical macroautophagic pathways. Instead, the selective uptake may be similar to other protein sorting pathways such as protein translocation through the endoplasmic reticulum or protein import into mitochondria.
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PMID:Lysosomal degradation of microinjected proteins. 270 96

Free amino acid contents in skin extracts and influence of food and starvation on free amino acid content in skin mucus were analysed in sexually immature goldfish. Free amino acid concentration in skin mucus (91.1 mumol/g dry wt) was higher than in deep skin (54 mumol/g) or in whole skin (56.6 mumol/g) extracts. Free amino acid compositions were very similar in the latter extracts. They both differed from skin mucus extract in taurine, glutamic acid, glycine and histidine relative contents. Free amino acid composition in zooplankton used to feed goldfish was close to the composition found in corresponding skin mucus extracts, except in taurine content. Goldfish weighing 3 g (6 months old) and 17 g (1 year old) reared on zooplankton showed similar patterns of free amino acid composition in skin mucus. Comparison with free amino acid composition in skin mucus from goldfish fed on commercial food had big differences in glutamic acid, valine, methionine and lysine relative contents. During fasting, we observed an increase in the amount of mucus secreted and a concomitant decrease of the free amino acid concentration in the secretion. The origin of free amino acids found in skin mucus and their possible role in pheromonal and allelochemical communications of goldfish are discussed.
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PMID:Free amino acid content in the skin mucus of goldfish, Carassius auratus L.: influence of feeding. 286 12

During asparagine starvation the frequency of lysine for asparagine substitutions increases to levels that enable one to isolate and sequence mistranslated protein. We have used site-directed mutagenesis to construct a series of derivatives of the gene encoding the coat protein of the bacteriophage MS2. The mutant set constructed has either AAU or AAC as codon three in the gene with each possible adjoining 3' base. Lysine incorporation in coat protein encoded by these genes shows that AAU is misread from 4- to 9-fold more frequently than AAC with any 3' context. Although in some cases context effects of approximately 2-fold were noted, there seems to be no simple hypothesis to explain them.
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PMID:Missense misreading of asparagine codons as a function of codon identity and context. 311 58

The plasmid gene cat-86 is induced by chloramphenicol in Bacillus subtilis, resulting in the synthesis of the gene product chloramphenicol acetyltransferase. Induction is due to a posttranscriptional regulatory mechanism in which the inducer, chloramphenicol, activates translation of cat-86 mRNA. We have suggested that chloramphenicol allows ribosomes to destabilize a stem-loop structure in cat-86 mRNA that sequesters the ribosome-binding site for the coding sequence. In the present report we show that cat-86 expression can be activated by stalling ribosomes in the act of translating a regulatory leader peptide. Stalling was brought about by starving host cells for specific leader amino acids. Ribosomal stalling, which led to cat-86 expression, occurred upon starvation for the amino acid specified by the leader codon located immediately 5' to the RNA stem-loop structure and was independent of whether that codon specified lysine or tyrosine. These observations support a model for chloramphenicol induction of cat-86 in which the antibiotic stalls ribosome transit in the regulatory leader. Stalling of ribosomes in the leader can therefore lead to destabilization of the RNA stem-loop structure.
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PMID:Drug-free induction of a chloramphenicol acetyltransferase gene in Bacillus subtilis by stalling ribosomes in a regulatory leader. 311 38

By using the Cu2+ method (Y. Ohsumi, K. Kitamoto, and Y. Anraku, J. Bacteriol. 170:2676-2682, 1988) for differential extraction of the vacuolar and cytosolic amino acid pools from yeast cells, the amino acid compositions of the two pools extracted from Saccharomyces cerevisiae cells, grown in synthetic medium supplemented with various amino acids, were determined. Histidine and lysine in the medium expanded the vacuolar pool extremely. Glutamate also accumulated in the cells, but mainly in the cytosol. The composition of amino acids in the cytosolic pool was fairly constant, in contrast to that in the vacuolar pool. Cells grown in synthetic medium supplemented with 10 mM arginine accumulated arginine in the vacuoles at a concentration of about 430 mM. This large arginine pool was metabolically active and was effectively utilized during nitrogen starvation. Arginine efflux from the vacuoles was coupled with K+ influx, with an arginine/K+ exchange ratio of 1, as judged by the initial rate. The vacuolar arginine pool was exchangeable with lysine added to the medium and was decreased by treatment of the cells with the mating pheromone, alpha-factor.
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PMID:Dynamic aspects of vacuolar and cytosolic amino acid pools of Saccharomyces cerevisiae. 313 4

Brief starvation is accompanied by decreased circulating levels of most amino acids, which has been attributed to an increased splanchnic uptake of amino acids, primarily alanine, for gluconeogenesis. However, quantitative data on splanchnic exchange of amino acids and gluconeogenic precursors is lacking. Consequently, arterial concentrations and splanchnic exchange of whole blood amino acids, ketone bodies, glucose, and gluconeogenic precursors were measured in 16 prolonged fasted (60 to 64 hours) and 15 overnight fasted (12 to 14 hours) healthy, nonobese subjects. After the 60-hour fast net splanchnic glucose production decreased by 41% to 0.31 +/- 0.02 mumol/L (P less than .001), whereas the splanchnic uptake of gluconeogenic precursors increased and could account for the total glucose output. Net splanchnic uptake of taurine, threonine, serine, glycine, lysine, histidine, and arginine rose significantly in response to fasting (P less than .05 to .01) due to increased splanchnic fractional extraction. Although the splanchnic fractional extraction of alanine was augmented by 40% (P less than .001), net splanchnic uptake was not influenced by fasting. Total net splanchnic uptake of amino acids increased by 68%, from 231 +/- 44 mumol/min in the postabsorptive state to 388 +/- 63 mumol/min (mean +/- SEM) (P less than .05) in the 60-hour fasted state. However, only one half of this rise was accounted for by gluconeogenic amino acids.
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PMID:Splanchnic metabolism of amino acids in healthy subjects: effect of 60 hours of fasting. 319 1


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