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PubMed1973

Lysis of Escherichia coli by glycine is potentiated by pyridoxine starvation.

Pyridoxineless mutants of Escherichia coli are lysed in a few hours when starved for pyridoxine in a glucose minimal medium containing glycine at 10 mM. The lysis is prevented equally well by l-alanine and by d-alanine when either is present at 0.1 mM. The lysis is potentiated by 0.5 mM l-methionine. The peculiar susceptibility of E. coli B to glycine-mediated lysis during starvation for pyridoxine suggests that the starvation reduces the availability of some normal antagonist of glycine, presumably alanine.

Alanine↗
PubMed1973

Effect of isoleucine, valine, or leucine starvation on the potential for formation of the branched-chain amino acid biosynthetic enzymes.

The derepression of the isoleucine and valine biosynthetic enzymes in Escherichia coli and Salmonella typhimurium was examined under conditions of restriction of isoleucine, valine, or leucine (the three amino acids needed for multivalent repression of these enzymes). A procedure was used that allowed the measurement of enzyme-forming potential that accumulated during the starvation period, but could not be expressed unless the missing amino acid was supplied. The threonine deaminase (the product of the ilvA gene)-forming potential that accumulated under such conditions was found to be unstable and decayed with a half-life of about 2.5 min (at 37 C). Evidence was obtained that indicates the threonine deaminase-forming potential that accumulates under conditions of isoleucine starvation is in the form of initiated (rifampin-resistant), but uncompleted (actinomycin D-sensitive), messenger ribonucleic acid chains. Furthermore, it appears that a large portion of the threonine deaminase- and dehydrase (the product of the ilvD gene)-forming potential, under such conditions, is in the form of initiated polypeptide chains. Based on these results and results obtained with SuA(-) strains, a model is presented that explains how the second gene (D) in the ilvADE operon can be partially transcribed and translated under conditions in which there are no completed messenger ribonucleic acids for the gene (A) transcribed before it.

Bacterial Proteins↗
PubMed1973

Death resulting from fatty acid starvation in yeast.

Mutants of Saccharomyces cerevisiae having the genotypes fas1 (fatty acid synthetase minus) and fas1, ole1 (fatty acid synthetase and fatty acid desaturase minus) were found to undergo logarithmic death when deprived of required fatty acids, whereas ole1 strains did not. During the first 2 to 3 h of fatty acid starvation, macromolecular synthesis occurred at apparently normal rates, although cell division stopped by the end of the 1st h. Cell death commenced at approximately the 2nd to the 3rd h, and within 24 h, depending upon conditions, 2 to 4 log orders of death had occurred. The loss of viability was accelerated by the addition of detergent, but could be largely prevented by the interruption of protein synthesis, either by amino acid starvation or by the use of cycloheximide. The possible significance of this phenomenon in terms of membrane biosynthesis is discussed.

Arginine↗
PubMed1975

Formation of chromatographically unique species of transfer ribonucleic acid during amino acid starvation of relaxed-control Escherichia coli.

Examination of the transfer ribonucleic acid (tRNA) produced by starving, relaxed-control (rel minus) strains of Escherichia coli for required amino acids revealed the occurrence of a number of chromatographically unique subspecies. Leucine starvation results in the formation of new isoacceptor species of leucine-, histidine-, arginine-, valine-, and phenylalanine-specific tRNA and quantitative changes in the column profiles of serine, glycine, and isoleucine tRNA. Evidence that the unique tRNA species are synthesized de novo during amino acid starvation comes from the findings that the major unique leucine isoacceptor species is not formed in stringent control cells or in rel minus cells starved for uracil or treated with rifampin. Furthermore, heat treatment of the unique leucine tRNA does not alter its chromatographic behavior, indicating that the species is not an aggregate or nuclease-damaged form of a normal isoacceptor tRNA. The methyl acceptor activities of tRNA from leucine-starved and nonstarved rel+ or rel minus cells were found to be essentially the same. This result and the finding that the chromatographic behavior of the unique leucine-specific tRNA was not altered after treatment with tRNA methylase suggests that gross methyl deficiency is probably not the biochemical basis for the occurrence of the unique species.

Acylation↗
PubMed1975

Production of cells without deoxyribonucleic acid during thymidine starvation of lexA- cultures of Escherichia coli K-12.

When thymidine-requiring lexA- strains were starved for thymidine, the kinetics of survival were similar to those of a nearly isogenic lexA+ strain. The size distribution of cells in the lexA- and lexA+ cultures were, however, quite different. Whereas most of the cells in the starved lexA+ cultures grew into long filamentous forms (longer than 4.0 mum), many of the lexA- cells were found to have a normal rod shape (4.0 mum or shorter). It was shown that lexA- cells undergo more divisions during thymidine starvation than lexA+ cells. Furthermore, using an autoradiographic method to analyze deoxyribonucleic acid (DNA) distribution in the starved cells, we demonstrated that cells without DNA are produced in both normal and starved lexA- cultures at a much higher frequency than in lexA+ cultures. Some of these cells may be produced by breakdown of DNA, but we favor the hypothesis that they result from an abnormal cell division process. Since lexA mutations are dominant, we conclude that a diffusible product decreases the synthesis or activity of an inhibitor of cell division in lexA- strains when DNA synthesis is blocked by thymidine starvation.

Cell Count↗
PubMed1977

Control of cell division in Escherichia coli: effect of amino acid starvation.

The effect of amino acid starvation on cell division was studied in cells of Escherichia coli B. In this bacterial strain, deprivation of a required amino acid resulted in synchronous cell division upon restoration of the amino acid. This synchronization was apparently due to a shift forward in the cell cycle during the starvation. As a consequence, the cells divided at a size that was smaller than normal.

Amino Acids↗
PubMed1977

Growth and cell division during nitrogen starvation of the yeast Saccharomyces cerevisiae.

During nitrogen starvation, cells of the yeast Saccharomyces cerevisiae increased threefold in number, and little ribonucleic acid (RNA) and protein were accumulated. Both RNA and protein were extensivley degraded during starvation, suggesting that intracellular macromolecules could supply most of the growth requirements. The types and proportions of stable RNA synthesized during nitrogen deprivation were characteristic of exponentially growing cells; however, the complement of proteins synthesized was different. We conclude that, once events in the deoxyribonucleic acid division cycle are initiated, cells can complete division with little dependence on continued net cell growth.

Cell Division↗
PubMed1978

Noncoordinate control of RNA, lipopolysaccharide, and phospholipid syntheses during amino acid starvation in stringent and relaxed strains of Escherichia coli.

The syntheses of RNA, lipopolysaccharides, and phospholipids were measured simultaneously in stringent and relaxed cells of Escherichia coli during normal growth or starvation for amino acids. The synthesis of all these molecules was inhibited by amino acid starvation, but the reduction in synthesis was not coordinated.

Amino Acids↗
PubMed1978

Ligninolytic enzyme system of Phanaerochaete chrysosporium: synthesized in the absence of lignin in response to nitrogen starvation.

The relationship between growth, nutrient nitrogen assimilation, and the appearance of ligninolytic activity was examined in stationary batch cultures of the wood-destroying hymenomycete Phanerochaete chrysosporium Burds. grown under conditions optimized for lignin metabolism. A reproducible sequence of events followed inoculation: 0 to 24 h, germination, linear growth, and depletion of nutrient nitrogen; 24 to 48 h, cessation of linear growth and derepression of ammonium permease activity (demonstrating nitrogen starvation); 72 to 96 h, appearance of ligninolytic activity (synthetic 14C-lignin leads to 14CO2). Experiments with cycloheximide demonstrated that appearance of ligninolytic activity occurs irrespective of the presence of lignin; lignin did not induce additional activity. Addition of NH4+ to cultures immediately prior to the time of appearance of the ligninolytic system delayed its appearance, suggesting that the NH4+ led to interference with synthesis of the enzyme system. Addition of NH4+ to ligninolytic cultures resulted in an eventual, temporary decrease in ligninolytic activity. The results suggest that all or essential protein components of the ligninolytic enzyme system are synthesized as part of a series of physiological ("secondary metabolic") events that are initiated by nutrient nitrogen starvation.

Basidiomycota↗
PubMed1980

Effects of inositol starvation on phospholipid and glycan syntheses in Saccharomyces cerevisiae.

The early biochemical consequences of inositol starvation in an inositol auxotroph of Saccharomyces cerevisiae were examined as a means of determining the cellular role of inositol. Upon withdrawal of inositol, the rate of incorporation of 32P-labeled inorganic phosphate into phosphatidylinositol and into the phosphoinositol-containing sphingolipids immediately dropped by 80 and 50%, respectively; however, synthesis of the other major phospholipids continued for 2 to 3 h at control rates. The incorporation of [U-14C]glucose into cell wall glycans began to decline immediately poststarvation and decreased to 50% of the initial rate by 80 min for mannan and by 140 min for alkali- and acid-insoluble glucan. These changes in the rates of synthesis of cell wall glycan and phosphatidylinositol were the earliest effects of inositol starvation, preceding inhibition of the synthesis of protein and ribonucleic acid as measured by incorporation of radioactive precursors into trichloroacetic acid-insoluble cell material. These results suggest that phosphatidylinositol may play a direct role in the synthesis or secretion of yeast glycans.

Fungal Proteins↗
PubMed1981

Branched-chain amino acid fermentation by a marine spirochete: strategy for starvation survival.

An anaerobic marine spirochete (strain MA-2) fermented glucose and formed ethanol, acetic acid, CO(2), and H(2) as end products. The organism required carbohydrates as growth substrates. Amino acids did not support the growth of strain MA-2. However, when the spirochete was grown in media containing branched-chain amino acids and glucose, significant quantities of 4- and 5-carbon branched-chain volatile fatty acids were formed in addition to products of glucose fermentation. Smaller quantities of branched-chain alcohols were also formed under these conditions. The spirochete converted l-valine, l-isoleucine, and l-leucine to isobutyric, 2-methylbutyric, and isovaleric acids, respectively. CO(2) formation accompanied each of these conversions. Spirochete MA-2 did not require branched-chain amino acids for growth, but these compounds could serve as sole sources of nitrogen for the organism. In addition, the survival of starving cells (no growth substrate available) of spirochete MA-2 was prolonged significantly when l-valine, l-isoleucine, and l-leucine were present in starvation media. Starving cells fermented these amino acids, forming adenosine 5'-triphosphate and branched-chain fatty acids. Our findings indicate that energy derived from amino acid fermentation allows the spirochete to survive periods of growth substrate starvation. Apparently, dissimilation of branched-chain amino acids can provide this bacterium with maintenance energy for cell functions not related to growth. In its natural environment spirochete MA-2 may catabolize branched-chain amino acids as a strategy for survival when growth substrates are not available.

Adenosine Triphosphate↗
PubMed1984

Role of inositol-containing sphingolipids in Saccharomyces cerevisiae during inositol starvation.

The in vitro lipid requirements of UDP-N-acetylglucosamine-dolichol phosphate N-acetylglucosamine-1-phosphotransferase for the inositol-containing sphingolipids from Saccharomyces cerevisiae were characterized in terms of concentration and specificity. The effects of combinations of lipids, especially phosphatidylinositol and the inositol-containing sphingolipids, were also tested on the transferase. Phosphatidylinositol and phosphatidylglycerol stimulated the enzyme 3.3- and 2.8-fold, respectively. The inositol-containing sphingolipids, phosphatidylcholine, phosphatidylethanolamine, and phosphatidylserine did not stimulate the activity of the transferase. Phosphatidylcholine and phosphatidylethanolamine in combination with phosphatidylinositol had no effect on the transferase activity; however, the inositol-containing sphingolipids markedly inhibited the stimulation of the transferase by phosphatidylinositol. This inhibition by the sphingolipids was prevented if phosphatidylcholine, in addition to the other lipids, was present in the assay mixture. In addition, changes due to inositol starvation in the in vivo membrane lipid environment, i.e., phosphatidylinositol and the inositol-containing sphingolipids, were analyzed to determine whether they corresponded to the observed in vitro effects. Three hours after the beginning of inositol starvation, there were 9- and 14-fold reductions in the accumulation of phosphatidylinositol in membrane fractions IIA (vesicles) and IV (endoplasmic reticulum), respectively, although there was only a 6-fold reduction in membrane fraction I (plasma membrane). The accumulation of [14C]inositol into inositol-containing sphingolipids also reflected the differences in the cellular location of membranes.

Cell Membrane↗
PubMed1986

Phosphate starvation regulon of Salmonella typhimurium.

Several phosphate-starvation-inducible (psi) genetic loci in Salmonella typhimurium were identified by fusing the lacZ gene to psi promoters by using the Mu d1 and Mu d1-8 bacteriophages. Although several different starvation conditions were examined, the psi loci responded solely to phosphate deprivation. A regulatory locus, psiR, was identified as controlling the psiC locus. The psiR locus did not affect the expression of the Escherichia coli phoA locus or any of the other psi loci described.

Chromosome Mapping↗
PubMed1989

Changes in polypeptide composition of Synechocystis sp. strain 6308 phycobilisomes induced by nitrogen starvation.

Phycobilisomes isolated from actively growing Synechocystis sp. strain 6308 (ATCC 27150) consist of 12 polypeptides ranging in molecular mass from 11.5 to 95 kilodaltons. The phycobilisome anchor and linker polypeptides are glycosylated. Nitrogen starvation causes the progressive loss of phycocyanin and allophycocyanin subunits with molecular masses between 16 and 20 kilodaltons and of two linker polypeptides with molecular masses of 27 and 33 kilodaltons. Nitrogen starvation also leads to enrichment of four additional polypeptides with molecular masses of 46, 53, 57, and 61 kilodaltons and a transient enrichment of 35- and 41-kilodalton polypeptides in isolated phycobilisomes. The 57-kilodalton additional polypeptide was identified by immunoblotting as the large subunit of ribulosebisphosphate carboxylase/oxygenase. Proteins with the same molecular weights as the additional polypeptides were also coisolated with the 12 phycobilisome polypeptides in the supernatant of nitrogen-replete Synechocystis thylakoid membranes extracted in high-ionic-strength buffer and washed with deionized water. These observations suggest that the additional polypeptides in phycobilisomes from nitrogen-starved cells may be soluble or loosely bound membrane proteins which associate with phycobilisomes. The composition and degree of association of phycobilisomes with soluble and adjacent membrane polypeptides appear to be highly dynamic and specifically regulated by nitrogen availability. Possible mechanisms for variation in the strength of association between phycobilisomes and other polypeptides are suggested.

Blotting, Western↗
PubMed1990

Starvation-induced cross protection against osmotic challenge in Escherichia coli.

Stationary-phase Escherichia coli cultures showed enhanced osmotic resistance as compared with cultures in mid-logarithmic growth or preadapted to osmotic stress. The osmotolerance that developed during starvation or osmotic adaptation required de novo protein synthesis. Of the 22 polypeptides induced during osmotic shock, five were also starvation proteins.

Bacterial Proteins↗
PubMed1994

Role of the transcriptional activator AppY in regulation of the cyx appA operon of Escherichia coli by anaerobiosis, phosphate starvation, and growth phase.

Transcriptional lacZ fusions have been used to analyze the regulation of the appA operon of Escherichia coli. The appA operon contains the genes cyxA and cyxB, coding for the putative third cytochrome oxidase, and appA, encoding acid phosphatase. The analysis showed that the cyxAB and the appA genes are cotranscribed from a potentially strong promoter, Pcyx, located immediately upstream of cyxA and that the operon in addition contains an internal promoter, PappA, contributing significantly to the transcription of the appA gene. The two promoters were both induced by starvation for Pi and by entry into stationary phase. The cyx promoter was in addition found to be activated by anaerobic growth conditions. The product of the previously identified appY gene, which when present on a high-copy-number plasmid stimulates synthesis of acid phosphatase, was shown to activate the cyx promoter. An insertion mutation in the appY gene was constructed in vitro and recombined into the chromosome. The appY mutation eliminated induction of the cyx promoter by anaerobiosis and severely reduced induction of this promoter by phosphate starvation and upon entry into stationary phase but had no effect on induction of the appA promoter. The appY mutation had no effect on survival in stationary phase, nor did it have any effect on growth rate or yield under aerobic or anaerobic conditions. The possibility that AppY is a third global regulator of energy metabolism genes is discussed.

Anaerobiosis↗
PubMed1997

Bacillus subtilis PhoP binds to the phoB tandem promoter exclusively within the phosphate starvation-inducible promoter.

Several gene products, including three two-component systems, make up a signal transduction network that controls the phosphate starvation response in Bacillus subtilis. Epistasis experiments indicate that PhoP, a response regulator, is furthest downstream of the known regulators in the signaling pathway that regulates Pho regulon genes. We report the overexpression, purification, and use of PhoP in investigating its role in Pho regulon gene activation. PhoP was a substrate for both the kinase and phosphatase activities of its cognate sensor kinase, PhoR. It was not phosphorylated by acetyl phosphate. Purified phosphorylated PhoP (PhoPP) had a half-life of approximately 2.5 h, which was reduced to about 15 min by addition of the same molar amount of *PhoR (the cytoplasmic region of PhoR). ATP significantly increased phosphatase activity of *PhoR on PhoPP. In gel filtration and cross-linking studies, both PhoP and PhoPP were shown to be dimers. The dimerization domain was located within the 135 amino acids at the N terminus of PhoP. Phosphorylated or unphosphorylated PhoP bound to one of the alkaline phosphatase gene promoters, the phoB promoter. Furthermore, PhoP bound exclusively to the -18 to -73 region (relative to the transcriptional start site +1) of the phosphate starvation-inducible promoter (Pv) but not to the adjacent developmentally regulated promoter (Ps). These data corroborate the genetic data for phoB regulation and suggest that activation of phoB is via direct interaction between PhoP and the phoB promoter. Studies of the phosphorylation, oligomerization, and DNA binding activity of the PhoP protein demonstrate that its N-terminal phosphorylation and dimerization domain and its C-terminal DNA binding domain function independently of one another, distinguishing PhoP from other response regulators, such as PhoB (Escherichia coli) and NtrC.

Bacillus subtilis↗