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)

Guanine auxotrophs of Escherichia coli K-12 were isolated after mutagenesis with N-methyl-N'-nitro-N-nitrosoguanidine, ethyl methane sulfonate, or the acridine mustard ICR 372. guaA (xanthosine 5'-monophosphate [XMP] aminase-less) mutants were distinguished from guaB (inosine 5'-monophosphate [IMP] dehydrogenase-less) mutants by their growth response to xanthine and by enzyme assay. Mutations were classified as base substitutions or frameshift on the basis of mutagen-induced reversion patterns. All guaA strains, including three frameshift mutants, produced derepressed levels of IMP dehydrogenase when cultured with a growth-limiting concentration of guanine. The guaB strains were of two types: (i) those producing derepressed levels of XMP aminase, and (ii) those producing basal levels of XMP aminase when grown under conditions of guanine starvation. In the guaB strains of the second type, the expression of the adjacent guaA gene is reduced. It is proposed that this pleiotropic effect of some guaB mutations is a result of polarity. The orientation of polarity suggests the gene order "operator"-guaB-guaA. Gel diffusion studies with IMP dehydrogenase antiserum showed that strains carrying polar guaB mutations do not produce cross-reacting material (CRM). The remaining guaB mutants were either CRM(+) or CRM(-). Mapping the mutations by three-factor crosses showed that polar and nonpolar guaB sites are clustered in a small genetic region cotransducible with guaA. The relative positions of the guaB mutational sites established that the polar mutations lie within the structural gene for IMP dehydrogenase.
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PMID:The gua operon of Escherichia coli K-12: evidence for polarity from guaB to guaA. 435 75

Bacillus subtilis cells were exposed to decoyinine to trigger stringent transcription control through inhibition of GMP synthase; amino acid starvation results in the same control through inhibition of GMP kinase by 5'-diphosphate 3'-diphosphate guanosine. The positive and negative transcription control of the stringent genes involves adenine and guanine at the transcription initiation sites, whereby they sense an increase and a decrease in the in vivo ATP and GTP pools, respectively. Decoyinine also induces sporulation in minimum medium. DNA microarray analysis revealed that decoyinine induced two major sensor kinase genes, kinA and kinB, involved in the phosphorelay leading to spore formation. lacZ fusion experiments involving the core promoter regions of kinA and kinB, whose transcription initiation bases are adenines, indicated that decoyinine induced their expression. This induction was independent of CodY and AbrB. When the adenines were replaced with guanines or cytosines, the induction by decoyinine decreased. The in situ replacement of the adenines with guanines actually affected this decoyinine-induced sporulation as well as massive sporulation in nutrient medium. These results imply that operation of the positive stringent transcription control of kinA and kinB, which is mediated by an increase in the ATP pool, is likely a prerequisite for the phosphorelay to transfer the phosphoryl group to Spo0A to initiate sporulation.
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PMID:Expression of kinA and kinB of Bacillus subtilis, necessary for sporulation initiation, is under positive stringent transcription control. 2337 9