Occurrence of guanosine-5'-diphosphate-3'-diphosphate and adenosine-5'-triphosphate-3'-diphosphate in Streptomyces galilaeus.
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منابع مشابه
In vitro degradation of guanosine 5'-diphosphate, 3'-diphosphate.
The degradation of guanosine 5'-diphosphate,3'-diphosphate (ppGpp) by the "crude" ribosomal fraction of Escherichia coli CP78 (rel+, spoT+) was demonstrated and characterized. When the 3'-pyrophosphoryl group of ppGpp was hydrolyzed, the primary degradation product was 5'-GDP. Phosphorylation of ppGpp to guanosine 5'-triphosphate,3'-diphosphate (pppGpp) prior to degradation was not necessary. T...
متن کاملEnergy deprivation and guanosine 5'-diphosphate 3'-diphosphate synthesis in cyanobacteria.
A reduction in the incident light intensity has been used to elicit guanosine 5'-diphosphate 3'-diphosphate accumulation in cyanobacteria. Inhibitors of photophosphorylation, 2,4-dinitrophenol, and carbonyl cyanide-m-chlorophenyl hydrazone elicited accumulation in three species of cyanobacteria when they were grown on dinitrogen or nitrate, but not in cultures grown on ammonium or glutamine. Ac...
متن کاملMechanism of the in vitro breakdown of guanosine 5'-diphosphate 3'-diphosphate in Escherichia coli.
Degradation of guanosine tetraphosphate (ppGpp) involves an enzyme associated with the ribosomal fraction from spoT+ strains of Escherichia coli. Double-label experiments with pp[3h]gpp, pp[3H]Gpp, or pp[3H]Gpp as substrate strongly suggest that ppG is the degradation product and that the enzyme releases two phosphates coordinately from the 3' position of ppGpp. In the absence of pppA this reac...
متن کاملProtein synthesis results in guanosine-5'-diphosphate-3'-diphosphate synthesis in Escherichia coli minicells.
Minicells of Escherichia coli DS410 synthesized guanosine-5'-diphosphate-3'-diphosphate and guanosine-5'-triphosphate-3'-diphosphate when synthesizing proteins in response to phage T7 infection. The guanosine-5'-diphosphate-3'-diphosphate synthesis was found to be relA+ dependent and inhibited by chloramphenicol.
متن کاملChanges in the concentrations of guanosine 5'-diphosphate 3'-diphosphate and the initiating nucleoside triphosphate account for inhibition of rRNA transcription in fructose-1,6-diphosphate aldolase (fda) mutants.
Early screens for conditional lethal mutations that affected rRNA expression in Escherichia coli identified temperature-sensitive fda mutants (fda encodes the glycolytic enzyme fructose-1,6-diphosphate aldolase). It was shown that these fda(Ts) mutants were severely impaired in rRNA synthesis upon shift to the restrictive temperature, although the mechanism of inhibition was never determined. H...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1980
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.44.1003