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

The physiological and genetic controls operating on phosphate-regulated promoters were studied in greater detail. This was done by defining the control for three phosphate-regulated genes: phoA, psiE, and psiO. Each is highly inducible by phosphate starvation. Individually, these phosphate-starvation-inducible, psi, genes at the same time show common and differing features in their molecular control. The phoA gene, encoding alkaline phosphatase, is specifically induced by phosphate starvation. It is negatively controlled by phoR as well as by the phosphate-specific transport (PST) system in Escherichia coli. phoA induction is positively controlled by the phoB, M, and R products; it is unaffected by the cAMP and CAP system. The psiE and psiO genes were studied by using strains with lacZ fused to their respective promoters. psiE-lacZ is induced by phosphate-, carbon- or nitrogen-limited growth. Genetically, psiE-lacZ induction is partially phoB and phoR-dependent. However, its expression is phoM-independent. This implies that phoB/phoR coupled control differs from phoB/phoM coupled control. Repression of psiE-lacZ is substantially altered in only some PST mutants, such as phoT. In addition, psiE-lacZ is negatively controlled by the cAMP and CAP system. psiO-lacZ is induced by phosphate-, carbon- or nitrogen-limited growth or by anaerobiosis. Its expression is unaffected by any pho mutation that has been previously described. A cell density-dependent induction of psiO-lacZ is observed in lon mutants. Also, psiO-lacZ is negatively controlled by the cAMP-CAP system. In summary, these results demonstrate that co-ordinately regulated promoters can have some common regulatory elements while, at the same time, not sharing other controlling factors.
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PMID:Overlapping and separate controls on the phosphate regulon in Escherichia coli K12. 630 24

phoB is a positive regulatory gene for phoA, which codes for alkaline phosphatase, as well as for other genes belonging to the phosphate (pho) regulon whose expression is inducible by phosphate limitation in Escherichia coli. A hybrid plasmid that contains a phoB-lacZ fused gene was constructed in vitro. This plasmid enabled us to study phoB gene expression by measuring the beta-galactosidase level in the cells. The plasmid was introduced into various regulatory mutants related to the phosphate regulon, and phoB gene expression in these strains was studied under limited and excess phosphate conditions. It was found that the regulation of phoB expression was very similar to that of phoA expression. Expression of both genes was induced by phosphate starvation. Both genes were constitutively expressed in phoR, phoS, phoT and phoU mutants and were not expressed in a phoR-phoM double mutant. The implications of these findings for the regulatory mechanism of the pho regulon are discussed.
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PMID:Regulation of the pho regulon in Escherichia coli K-12. Genetic and physiological regulation of the positive regulatory gene phoB. 631 Jan 21

The phoB gene, which encodes a positive control factor for a number of phosphate-regulated genes in Escherichia coli, was cloned into multicopy plasmid pBR322. A phoB-cat fusion that expressed chloramphenicol transacetylase from the phoB promoter was constructed. Studies of the expression of the phoB-cat fusion showed that the pattern of regulation of the phoB gene was similar to that of the phoA gene, the structural gene for alkaline phosphatase. The phoB gene was derepressed under conditions of phosphate starvation, was constitutively expressed in a phoR background, and required the phoM gene product for expression in a phoR strain. Finally, a functional phoB product was required for its own synthesis. Our results indicate either that phoA gene expression responds directly to the concentration of the phoB gene product in cells or that the phoA and phoB controlling elements are quite similar.
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PMID:Analysis of regulation of phoB expression using a phoB-cat fusion. 631 14

The alkaline phosphatase of Plectonema boryanum shows a considerable increase in activity following placement of the cells in a phosphate free medium. Five days of phosphate starvation result in a 14-fold increase of alkaline phosphatase activity. Growth in the presence of inhibitors of transcription and translation indicate that the synthesis of the enzyme is de novo. Orthophosphate causes an immediate inhibition of enzyme activity. Enzyme was extracted from P. boryanum with lysozyme or polymyxin B treatment in order to make comparative studies of cell bound and cell free enzyme. Of several enzyme specific inhibitors tested, mercuric chloride was the most effective. Temperature studies showed that the cell bound enzyme was most active at 40 degrees C while the cell free enzyme was most active at 70 degrees C. The pH optimum was 9 for the cell free enzyme, and 8.8 for the cell bound. The enzyme was tested to determine if it could hydrolyse a number of different organic compounds. It hydrolysed p-nitrophenol phosphate 100%, fructose-6-phosphate 45%, beta-glycerol phosphate 25% and other compounds to a lesser degree. Of seventeen other Cyanobacteria tested for alkaline phosphatase, all were positive, and of these eleven were inducible for the enzyme. Ten of the isolates released some of the enzyme into the culture medium. Michaelis constants for the enzyme were also determined.
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PMID:Physiological aspects of alkaline phosphatase in selected cyanobacteria. 679 13

The localization of alkaline phosphomonoesterase (EC 3.1.3.1) was studied in two Pseudomonas species: P. maltophilia VKM B-591 and P. aeruginosa VKM B-889. The former species is characterized by constitutive synthesis of alkaline phosphatase, and its level is not regulated by orthophosphate in the medium. The enzyme of the latter species is orthophosphate-repressible. The two species differ also in the localization of the enzyme in the cell. Under the conditions of derepression (the absence of inorganic phosphate from the medium), the enzyme of the repressible strain of P. aeruginosa is actively synthesized on the membranes and secreted into the medium. Most of the enzyme activity (80--90%) is found in the cultural broth 4 h after phosphorus starvation. In P. maltophilia, 90% of the synthesized enzyme is found in the membrane fraction irrespective of the incubation time under the same conditions. Apparently, a correlation exists between the regulation of alkaline phosphatase synthesis and the localization of the enzyme. It is likely that in P. aeruginosa, just as in E. coli, alkaline phosphatase is synthesized on polysomes attached to the membrane, with the subsequent translocation of the enzyme to the site of its localization. P. maltophilia appears to have a defect in one of its membrane component responsible for the regulation of the synthesis and the secretion of the enzyme in the cell.
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PMID:[Relationship of Pseudomonas maltophilia alkaline phosphatase to its membranes]. 679 9

Studies were made on memory of the rhythmic change in activity of duodenal alkaline phosphatase in rats. During starvation, the peak enzyme activity decreased gradually disappearing in 4 days. The peak activity of duodenal alkaline phosphatase was retained by feeding starch diet for 4 days instead of starvation for 4 days, but not by feeding casein diet for the same period. Starvation for one day after feeding casein diet for 4 days resulted in disappearance of the peak activity. However, the peak activity was still retained after one day of starvation after 4 days on starch diet. Therefore, starch feeding appears to be important in the memory of the rhythmic change in activity of duodenal alkaline phosphatase.
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PMID:Memory of the rhythmic change in activity of duodenal alkaline phosphatase in rats. 686 51

A new form of alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) has been identified in the yeast Saccharomyces cerevisiae. Utilizing either synthetic or natural substrates, the enzyme exhibited a broad pH activity curve with maximum activity between 8.5 and 9.0. The enzyme was nonspecific with respect to substrate, attacking a variety of compounds containing phosphomonoester linkages, but has no detectable activity against polyphosphate, pyrophosphate or phosphodiester linkages. The enzyme exhibited an apparent Km of 0.25 mM with respect to p-nitrophenyl phosphate, 0.38 mM with respect to alpha-naphthyl phosphate, and 1.0 mM with respect to 5'AMP. The enzyme is regulated in a constitutive manner and its activity does not increase during phosphate starvation or sporulation, as does the repressible alkaline phosphatase. The enzyme is tightly bound to a particulate fraction of the cell, tentatively identified as the tonoplast membrane. It is not solubilized by treatment with high concentrations of NaCl, KH2PO4 or chaotropic agents. Triton X-100 (0.1%) solubilizes 12% of the particulate activity. This enzyme is differentiated from the other alkaline phosphatases found in yeast by its chromatographic elution DEAE-cellulose, kinetic parameters, heat stability and pH stability, as well as its particulate nature. This particulate alkaline phosphatase was found in every strain examined. It has a significantly lower specific activity in the phoH mutant and a higher activity in the acid phosphatase constitutive mutant A137.
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PMID:A particulate form of alkaline phosphatase in the yeast, Saccharomyces cerevisiae. 701 3

The ugp-dependent transport system for sn-glycerol-3-phosphate has been characterized. The system is induced under conditions of phosphate starvation and in mutants that are constitutive for the pho regulon. The system does not operate in membrane vesicles and is highly sensitive toward osmotic shock. The participation of a periplasmic binding protein in the transport process can be deduced from the isolation of transport mutants that lack the binding protein. As with other binding protein-dependent transport systems, this protein appears to be necessary but not sufficient for transport activity. The isolation of mutants has become possible by selection for resistance against the toxic analog 3,4-dihydroxybutyl-1-phosphonate that is transported by the system. sn-Glycerol-3-phosphate transported via ugp cannot be used as the sole carbon source. Strains have been constructed that lack alkaline phosphatase and glycerol kinase. In addition, they are constitutive for the glp regulon and contain high levels of glycerol-3-phosphate dehydrogenase. Despite the fact that these strains exhibit high ugp-dependent transport activity for sn-glycerol-3-phosphate they are unable to grow on it as a sole source of carbon. However, when cells are grown on an alternate carbon source, (14)C label from [(14)C]sn-glycerol-3-phosphate appears in phospholipids as well as in trichloroacetic acid-precipitable material. The incorporation of (14)C label is strongly reduced when sn-glycerol-3-phosphate is the only carbon source. In the presence of an alternate carbon source, this inhibition is relieved, and sn-glycerol-3-phosphate transported by ugp can be used as the sole source of phosphate.
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PMID:Characteristics of a binding protein-dependent transport system for sn-glycerol-3-phosphate in Escherichia coli that is part of the pho regulon. 704 85

A group of male rabbits was starved for 7 days. Their blood samples were collected, before and after the starvation period. Six rabbits were slaughtered for the recovery of livers, while the rest were refed for the next 7 days, at the end of which their blood samples were collected and livers taken out for various analyses. After 7 days of starvation, the total leukocytic count, haemoglobin, bilirubin, proteins and glucose contents, and activities of alkaline phosphatase and glutamate pyruvate transaminase of blood serum decreased significantly, while its lactate dehydrogenase activity and cholesterol, total lipids and urea contents showed a significant increase. In liver, except for the bilirubin and glucose contents, all the biochemical components--RNA, DNA and total proteins included--showed highly elevated values. Refeeding of the starved rabbits tended to normalize most within 7 days. Although RNA, DNA, total proteins, cholesterol and urea contents did not reach the normal level in liver during this period, they were definitely less than those of the starved condition. The hepatic transaminases activities and lipid content in starved + refed livers were considerably decreased during the refeeding period. The histological parameters were slow to recover.
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PMID:Effect of starvation and refeeding on the blood and liver of domesticated rabbits. 717 Sep 91

The yeast S. cerevisiae imports cytosolic components into the vacuole non-selectively by autophagy and degrades them by vacuolar hydrolases under nutrient starvation conditions. We developed a novel system for monitoring autophagy by constructing cells in which modified vacuolar alkaline phosphatase is expressed as an inactive precursor form in the cytosol. Under starvation conditions, the processing of the precursor to the mature form and phosphatase activity appeared gradually, and the mature form was located in the vacuole. Disruption of APG1, an essential gene for autophagy, resulted in no processing or phosphatase activity. These results indicate that the precursor form in the cytosol is transferred to the vacuole by autophagy and converted to the active form by vacuolar proteinases. Thus, autophagy could be determined easily and accurately by measuring the phosphatase activity.
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PMID:Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae. 774 31


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