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)

Transcription of the ARG4 gene of Saccharomyces cerevisiae is regulated by general control of amino acid biosynthesis but not by a specific regulatory mechanism. Three deletion mutants (delta I, delta II, delta III) successively removing DNA sequences upstream from the coding sequence have been phenotypically analyzed after insertion into a single copy plasmid. As expected, delta I, which lacks the sequences upstream to -155, including the two putative upstream activation sequences (UAS), was unable to derepress argininosuccinate lyase biosynthesis under conditions of amino acid starvation. In delta II (deleted up to -126) the enzyme activity was very low and cells harbouring this allele were arginine dependent. These drastic phenotypic changes can be attributed to the loss of 12 out of 14 dA residues from positions -124 to -137. This poly (dAdT) sequence most likely serves as an upstream promoter element for constitutive expression of ARG4. The delta III deletion removes all 5' sequences including the putative TATA box. This inactive allele has been successfully used for selecting yeast promoters of unknown origin.
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PMID:Deletion analysis of the ARG4 promoter of Saccharomyces cerevisiae: a poly(dAdT) stretch involved in gene transcription. 227 87

The transcription and translation of operons for arginine biosynthetic enzymes after arginine removal (arginine down shift) were studied in relA and relA+ strains of Escherichia coli. After arginine down shift, derepression of synthesis of the arginine biosynthetic enzymes ornithine carbamoyltransferase (argF) and argininosuccinate lyase (argH) began at about 15 min in relA+ cells but was delayed in relA cells for more than 2 h. However, both relA+ and relA cells accumulated high levels of argCBH mRNA, as shown by dot blot hybridization, after arginine down shift. After 15 min of arginine limitation, the proportion of ribosome-bound argCBH mRNA was equivalent in both relA+ and relA cells. During the 15 min after the arginine down shift, relA+ cells produced a significant burst of argF and argH enzyme synthesis when arginine was added back to the culture, whereas relA cells did not produce this burst of enzyme synthesis. The relA cells regained the ability to produce a burst of argF and argH enzyme synthesis when alpha-methylglucose-induced glucose starvation was combined with arginine limitation. Significant guanosine 5'-diphosphate 3'-diphosphate accumulated in relA cells under this condition. Our results support the view that during periods of severe amino acid limitation guanosine 5'-diphosphate 3'-diphosphate acts in some way to ensure the translation of argCBH mRNA.
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PMID:Expression of arg genes of Escherichia coli during arginine limitation dependent upon stringent control of translation. 243 8

Argininosuccinate synthetase and argininosuccinate lyase catalyze the synthesis of arginine from citrulline in kidney and also serve as components of the urea cycle in liver of ureotelic animals. Dietary and hormonal regulation of mRNAs encoding these enzymes have been well studied in liver but not in kidney. Messenger RNAs for these enzymes are localized within the renal cortex. Starvation and extreme variations in dietary protein content (0% vs 60% casein) produced 2.6- to 3.5-fold increases in mRNA abundance for these two enzymes in rat kidney. Argininosuccinate lyase mRNA was not induced by dibutyryl cAMP, dexamethasone, or a combination of the two agents. In contrast, argininosuccinate synthetase mRNA was induced 2-fold by dibutyryl cAMP but was unresponsive to dexamethasone. Thus, diet and hormones regulate levels of these mRNAs in rat kidney, but the responses are both qualitatively and quantitatively distinct from the responses previously reported for rat liver.
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PMID:Nutritional and hormonal regulation of mRNA abundance for arginine biosynthetic enzymes in kidney. 254 41