Guanosine 5′-diphosphate 3′-diphosphate (ppGpp) as a negative modulator of polynucleotide phosphorylase activity in a ‘rare’ actinomycete
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چکیده
منابع مشابه
The Polymerization of Guanosine Diphosphate by Polynucleotide Phosphorylase
Polynucleotide phosphorylase catalyzes the reversible polymerization of nucleoside diphosphates (1). With enzyme preparations from Escherichia coli (2), Azotobacter agile (3), and Micrococcus lysodeikticus (4, 5) a reaction has been observed with single additions of adenosine, uridine, cytosine, or inosine diphosphate to form the corresponding homopolymer. However, the polymerization of guanosi...
متن کاملIn 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...
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Strain GS, a gram-negative motile bacterium isolated from soil, synthesizes two polysaccharides. The synthesis of a uranic acid-containing polysaccharide is derepressed by high concentrations of Na2SOd, while the synthesis of the polysaccharide containing equal quantities of n-rhamnose and n-talomethylose is repressed by NazS01 (1, 2). L-F’ucose and L-rhamnose are the methylpentoses commonly fo...
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.
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2010
ISSN: 0950-382X
DOI: 10.1111/j.1365-2958.2010.07240.x